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Zinc in PDB 6m2c: Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain

Enzymatic activity of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain

All present enzymatic activity of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain:
2.3.2.23; 2.3.2.24; 2.3.2.27;

Protein crystallography data

The structure of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain, PDB code: 6m2c was solved by S.O.Lee, K.S.Ryu, S.-W.Chi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.64 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.207, 141.241, 68.047, 90, 104.81, 90
R / Rfree (%) 21.2 / 25.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain (pdb code 6m2c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain, PDB code: 6m2c:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 6m2c

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Zinc binding site 1 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn401

b:27.6
occ:1.00
SG E:CYS326 2.3 34.9 1.0
SG E:CYS305 2.4 52.9 1.0
SG E:CYS302 2.5 33.5 1.0
SG E:CYS323 2.5 33.0 1.0
HB2 E:CYS326 2.8 28.2 1.0
HB3 E:CYS302 3.0 28.7 1.0
HB3 E:CYS305 3.1 31.2 1.0
H E:CYS305 3.1 31.4 1.0
CB E:CYS326 3.1 28.2 1.0
CB E:CYS302 3.2 28.7 1.0
H E:CYS323 3.2 31.0 1.0
CB E:CYS305 3.3 31.2 1.0
HB2 E:CYS302 3.4 28.7 1.0
HB3 E:CYS323 3.4 36.3 1.0
HB E:VAL304 3.5 27.6 1.0
CB E:CYS323 3.6 36.3 1.0
HB3 E:CYS326 3.6 28.2 1.0
N E:CYS305 3.7 31.4 1.0
H E:CYS326 3.8 33.1 1.0
HB2 E:SER308 4.0 38.2 1.0
N E:CYS323 4.0 31.0 1.0
CA E:CYS305 4.1 28.2 1.0
HB2 E:CYS305 4.1 31.2 1.0
CA E:CYS323 4.4 34.6 1.0
CA E:CYS326 4.4 28.4 1.0
HB2 E:CYS323 4.4 36.3 1.0
H E:VAL304 4.4 29.5 1.0
CB E:VAL304 4.4 27.6 1.0
N E:CYS326 4.4 33.1 1.0
H E:LEU306 4.6 28.4 1.0
HG E:SER308 4.6 44.1 1.0
H E:SER308 4.6 32.0 1.0
C E:VAL304 4.6 35.1 1.0
CA E:CYS302 4.7 33.5 1.0
HA E:SER322 4.7 29.7 1.0
HG E:SER307 4.7 44.5 1.0
HA E:CYS326 4.8 28.4 1.0
CB E:SER308 4.8 38.2 1.0
OG E:SER308 4.8 44.1 1.0
HE3 A:MET1 4.8 34.8 1.0
HA E:CYS305 4.8 28.2 1.0
H E:SER307 4.8 38.9 1.0
HG12 E:VAL304 4.9 18.4 1.0
C E:CYS305 4.9 31.2 1.0
O E:CYS323 4.9 36.3 1.0
CA E:VAL304 4.9 33.5 1.0
OG E:SER322 4.9 22.3 1.0
C E:CYS323 4.9 40.7 1.0
HG E:SER322 5.0 22.3 1.0
N E:VAL304 5.0 29.5 1.0
N E:LEU306 5.0 28.4 1.0

Zinc binding site 2 out of 8 in 6m2c

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Zinc binding site 2 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn402

b:33.3
occ:1.00
ND1 E:HIS319 2.0 33.7 1.0
SG E:CYS317 2.3 32.5 1.0
SG E:CYS339 2.3 38.2 1.0
SG E:CYS336 2.4 32.0 1.0
HB2 E:CYS317 2.6 34.6 1.0
CE1 E:HIS319 2.6 37.7 1.0
HE1 E:HIS319 2.8 37.7 1.0
CB E:CYS317 2.9 34.6 1.0
CG E:HIS319 3.0 35.4 1.0
HB2 E:HIS319 3.2 31.9 1.0
HB3 E:CYS336 3.2 37.4 1.0
CB E:CYS336 3.2 37.4 1.0
HB3 E:CYS317 3.2 34.6 1.0
HB2 E:CYS336 3.2 37.4 1.0
H E:CYS339 3.4 31.8 1.0
HB E:ILE338 3.5 37.1 1.0
CB E:HIS319 3.6 31.9 1.0
CB E:CYS339 3.7 34.5 1.0
HB3 E:CYS339 3.7 34.5 1.0
NE2 E:HIS319 3.7 41.0 1.0
CD2 E:HIS319 3.9 40.5 1.0
H E:HIS319 3.9 32.9 1.0
N E:CYS339 4.0 31.8 1.0
CA E:CYS317 4.3 39.6 1.0
HB3 E:HIS319 4.3 31.9 1.0
H E:ILE338 4.4 37.9 1.0
HB2 E:CYS339 4.4 34.5 1.0
HE2 E:HIS319 4.4 41.0 1.0
CA E:CYS339 4.4 30.7 1.0
N E:HIS319 4.4 32.9 1.0
CB E:ILE338 4.5 37.1 1.0
C E:CYS317 4.5 39.5 1.0
H E:GLN341 4.6 45.0 1.0
HB2 E:GLN341 4.6 40.7 1.0
HB2 E:PHE314 4.7 27.7 1.0
CA E:HIS319 4.7 30.9 1.0
CA E:CYS336 4.7 38.7 1.0
HD2 E:HIS319 4.7 40.5 1.0
H E:GLY318 4.8 31.6 1.0
HA E:CYS317 4.8 39.6 1.0
N E:GLY318 4.8 31.6 1.0
HD2 E:PHE314 4.8 30.5 1.0
HG3 E:GLN341 4.9 48.6 1.0
H E:CYS317 4.9 39.6 1.0
C E:ILE338 4.9 36.9 1.0
H E:ARG340 5.0 32.7 1.0
O E:CYS317 5.0 42.4 1.0

Zinc binding site 3 out of 8 in 6m2c

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Zinc binding site 3 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn401

b:38.2
occ:1.00
SG F:CYS323 2.3 43.5 1.0
SG F:CYS326 2.3 32.8 1.0
SG F:CYS302 2.3 30.6 1.0
SG F:CYS305 2.4 35.7 1.0
HB2 F:CYS326 2.9 28.3 1.0
HB3 F:CYS302 3.0 36.1 1.0
HB3 F:CYS305 3.0 34.6 1.0
H F:CYS323 3.0 38.4 1.0
CB F:CYS302 3.1 36.1 1.0
H F:CYS305 3.1 33.1 1.0
CB F:CYS326 3.2 28.3 1.0
HB3 F:CYS323 3.2 45.4 1.0
HB2 F:CYS302 3.2 36.1 1.0
CB F:CYS305 3.3 34.6 1.0
CB F:CYS323 3.3 45.4 1.0
HB F:VAL304 3.6 33.0 1.0
HB2 F:SER308 3.7 48.2 1.0
HB3 F:CYS326 3.7 28.3 1.0
N F:CYS305 3.7 33.1 1.0
H F:CYS326 3.8 38.6 1.0
N F:CYS323 3.8 38.4 1.0
HB2 F:CYS305 4.1 34.6 1.0
CA F:CYS305 4.1 32.8 1.0
CA F:CYS323 4.1 42.0 1.0
HB2 F:CYS323 4.1 45.4 1.0
CA F:CYS326 4.4 36.3 1.0
H F:VAL304 4.4 27.9 1.0
N F:CYS326 4.4 38.6 1.0
HG F:SER308 4.5 47.1 1.0
CB F:SER308 4.5 48.2 1.0
CB F:VAL304 4.6 33.0 1.0
CA F:CYS302 4.6 40.3 1.0
H F:SER308 4.6 42.3 1.0
H F:LEU306 4.6 37.2 1.0
O F:CYS323 4.6 44.6 1.0
OG F:SER308 4.7 47.1 1.0
C F:CYS323 4.7 45.3 1.0
C F:VAL304 4.7 34.6 1.0
HA F:SER322 4.7 36.6 1.0
HA F:CYS326 4.8 36.3 1.0
OG F:SER322 4.8 39.8 1.0
HA F:CYS305 4.9 32.8 1.0
HE1 B:MET1 4.9 30.1 1.0
HA F:CYS323 4.9 42.0 1.0
HG F:SER322 5.0 39.8 1.0
C F:CYS305 5.0 35.9 1.0
C F:SER322 5.0 42.8 1.0
H F:SER307 5.0 47.4 1.0
HA F:CYS302 5.0 40.3 1.0

Zinc binding site 4 out of 8 in 6m2c

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Zinc binding site 4 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn402

b:35.0
occ:1.00
SG F:CYS339 2.3 63.7 1.0
ND1 F:HIS319 2.4 38.6 1.0
SG F:CYS336 2.5 25.1 1.0
SG F:CYS317 2.5 33.9 1.0
HB2 F:CYS317 2.9 36.3 1.0
HB2 F:HIS319 3.0 38.8 1.0
HB3 F:CYS336 3.1 33.3 1.0
CB F:CYS336 3.2 33.3 1.0
CB F:CYS317 3.2 36.3 1.0
HB2 F:CYS336 3.2 33.3 1.0
CE1 F:HIS319 3.3 45.3 1.0
CG F:HIS319 3.3 43.2 1.0
H F:CYS339 3.4 36.3 1.0
HB3 F:CYS339 3.5 36.9 1.0
HE1 F:HIS319 3.5 45.3 1.0
HB3 F:CYS317 3.5 36.3 1.0
CB F:CYS339 3.6 36.9 1.0
HB F:ILE338 3.6 27.4 1.0
CB F:HIS319 3.6 38.8 1.0
N F:CYS339 3.9 36.3 1.0
H F:HIS319 4.0 31.6 1.0
HB3 F:HIS319 4.2 38.8 1.0
HD2 F:PHE314 4.2 32.6 1.0
HB2 F:CYS339 4.3 36.9 1.0
CA F:CYS339 4.4 40.0 1.0
H F:ILE338 4.4 35.2 1.0
NE2 F:HIS319 4.4 47.1 1.0
CD2 F:HIS319 4.4 50.5 1.0
CB F:ILE338 4.5 27.4 1.0
HB2 F:PHE314 4.5 34.1 1.0
HB2 F:GLN341 4.5 51.6 1.0
N F:HIS319 4.6 31.6 1.0
CA F:CYS317 4.6 36.0 1.0
HG22 F:ILE338 4.6 22.4 1.0
CA F:CYS336 4.7 36.8 1.0
CA F:HIS319 4.7 34.6 1.0
C F:ILE338 4.8 39.7 1.0
C F:CYS317 4.9 39.3 1.0
H F:GLN341 4.9 43.5 1.0
CG2 F:ILE338 5.0 22.4 1.0
HG21 F:ILE338 5.0 22.4 1.0

Zinc binding site 5 out of 8 in 6m2c

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Zinc binding site 5 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn401

b:29.6
occ:1.00
SG G:CYS326 2.2 30.2 1.0
SG G:CYS302 2.2 29.6 1.0
SG G:CYS323 2.3 30.9 1.0
SG G:CYS305 2.4 36.8 1.0
HB2 G:CYS326 2.8 31.9 1.0
HB3 G:CYS302 2.9 31.2 1.0
CB G:CYS302 3.0 31.2 1.0
H G:CYS305 3.1 38.6 1.0
CB G:CYS326 3.1 31.9 1.0
H G:CYS323 3.1 31.5 1.0
HB3 G:CYS305 3.2 38.8 1.0
HB2 G:CYS302 3.2 31.2 1.0
HB3 G:CYS323 3.3 32.9 1.0
CB G:CYS305 3.4 38.8 1.0
CB G:CYS323 3.4 32.9 1.0
HB3 G:CYS326 3.6 31.9 1.0
H G:CYS326 3.7 27.9 1.0
N G:CYS305 3.7 38.6 1.0
HB G:VAL304 3.8 32.4 1.0
HB2 G:SER308 3.8 41.1 1.0
N G:CYS323 3.9 31.5 1.0
CA G:CYS305 4.1 37.5 1.0
HB2 G:CYS305 4.2 38.8 1.0
CA G:CYS323 4.2 32.5 1.0
HB2 G:CYS323 4.2 32.9 1.0
H G:VAL304 4.3 36.0 1.0
CA G:CYS326 4.3 27.5 1.0
N G:CYS326 4.3 27.9 1.0
H G:SER308 4.4 37.3 1.0
H G:LEU306 4.5 39.9 1.0
CA G:CYS302 4.5 32.4 1.0
O G:CYS323 4.7 32.5 1.0
CB G:SER308 4.7 41.1 1.0
HA G:CYS326 4.7 27.5 1.0
CB G:VAL304 4.7 32.4 1.0
H G:SER307 4.7 40.9 1.0
HA G:SER322 4.7 31.5 1.0
C G:CYS323 4.7 34.2 1.0
C G:VAL304 4.8 36.7 1.0
HB2 G:GLU325 4.8 34.8 1.0
C G:CYS302 4.8 33.4 1.0
OG G:SER322 4.8 34.5 1.0
HG G:SER308 4.9 33.9 1.0
OG G:SER308 4.9 33.9 1.0
C G:CYS305 4.9 38.6 1.0
N G:LEU306 4.9 39.9 1.0
N G:VAL304 4.9 36.0 1.0
O G:CYS302 4.9 34.8 1.0
O G:HOH502 4.9 31.5 1.0
HA G:CYS305 4.9 37.5 1.0
HA G:CYS302 4.9 32.4 1.0
HG G:SER322 5.0 34.5 1.0

Zinc binding site 6 out of 8 in 6m2c

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Zinc binding site 6 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn402

b:43.6
occ:1.00
ND1 G:HIS319 2.1 38.1 1.0
SG G:CYS339 2.2 57.8 1.0
SG G:CYS317 2.4 50.2 1.0
HB2 G:CYS317 2.5 44.0 1.0
SG G:CYS336 2.5 29.8 1.0
CB G:CYS317 2.8 44.0 1.0
HB2 G:HIS319 2.9 39.2 1.0
CE1 G:HIS319 3.0 33.6 1.0
CG G:HIS319 3.1 42.5 1.0
HB3 G:CYS336 3.1 34.6 1.0
HE1 G:HIS319 3.1 33.6 1.0
HB3 G:CYS317 3.1 44.0 1.0
HB2 G:CYS336 3.1 34.6 1.0
CB G:CYS336 3.2 34.6 1.0
HB3 G:CYS339 3.4 50.0 1.0
CB G:HIS319 3.4 39.2 1.0
CB G:CYS339 3.5 50.0 1.0
H G:CYS339 3.6 37.7 1.0
HB G:ILE338 3.8 38.5 1.0
H G:HIS319 3.9 43.8 1.0
HB3 G:HIS319 4.0 39.2 1.0
N G:CYS339 4.1 37.7 1.0
NE2 G:HIS319 4.1 43.7 1.0
CD2 G:HIS319 4.2 45.3 1.0
HB2 G:CYS339 4.2 50.0 1.0
CA G:CYS317 4.3 41.8 1.0
HG3 G:GLN341 4.3 51.9 1.0
CA G:CYS339 4.4 36.7 1.0
HG2 G:GLN341 4.4 51.9 1.0
N G:HIS319 4.5 43.8 1.0
C G:CYS317 4.6 39.3 1.0
H G:ILE338 4.6 38.1 1.0
HB2 G:PHE314 4.6 34.1 1.0
CA G:HIS319 4.6 44.4 1.0
CA G:CYS336 4.7 36.6 1.0
H G:GLN341 4.7 48.6 1.0
HA G:CYS317 4.8 41.8 1.0
CB G:ILE338 4.8 38.5 1.0
HD2 G:PHE314 4.8 38.4 1.0
CG G:GLN341 4.8 51.9 1.0
H G:GLY318 4.9 39.3 1.0
HE2 G:HIS319 4.9 43.7 1.0
N G:GLY318 4.9 39.3 1.0
H G:CYS317 5.0 47.3 1.0
HG22 G:ILE338 5.0 42.8 1.0
O G:CYS317 5.0 42.0 1.0
C G:ILE338 5.0 44.5 1.0

Zinc binding site 7 out of 8 in 6m2c

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Zinc binding site 7 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn401

b:33.5
occ:1.00
SG H:CYS326 2.3 41.3 1.0
SG H:CYS302 2.3 31.1 1.0
SG H:CYS323 2.4 29.4 1.0
SG H:CYS305 2.5 52.1 1.0
HB3 H:CYS302 2.8 36.1 1.0
HB2 H:CYS326 2.9 31.9 1.0
HB3 H:CYS305 3.0 35.8 1.0
H H:CYS305 3.0 36.5 1.0
CB H:CYS302 3.0 36.1 1.0
HB2 H:CYS302 3.2 36.1 1.0
CB H:CYS326 3.2 31.9 1.0
CB H:CYS305 3.2 35.8 1.0
H H:CYS323 3.3 32.8 1.0
HB3 H:CYS323 3.4 30.4 1.0
HB H:VAL304 3.5 24.3 1.0
CB H:CYS323 3.6 30.4 1.0
HB2 H:SER308 3.6 36.9 1.0
N H:CYS305 3.6 36.5 1.0
HB3 H:CYS326 3.7 31.9 1.0
H H:CYS326 3.9 35.0 1.0
N H:CYS323 4.0 32.8 1.0
CA H:CYS305 4.0 38.4 1.0
HB2 H:CYS305 4.0 35.8 1.0
HG H:SER308 4.1 47.8 1.0
H H:VAL304 4.2 37.1 1.0
HB2 H:CYS323 4.3 30.4 1.0
CA H:CYS323 4.3 34.1 1.0
CA H:CYS326 4.4 35.0 1.0
CB H:VAL304 4.4 24.3 1.0
CA H:CYS302 4.5 35.9 1.0
CB H:SER308 4.5 36.9 1.0
H H:LEU306 4.5 44.2 1.0
N H:CYS326 4.5 35.0 1.0
H H:SER308 4.5 42.4 1.0
C H:VAL304 4.6 33.3 1.0
OG H:SER308 4.6 47.8 1.0
HA H:SER322 4.7 28.0 1.0
HA H:CYS305 4.8 38.4 1.0
HA H:CYS326 4.8 35.0 1.0
N H:VAL304 4.8 37.1 1.0
CA H:VAL304 4.8 34.9 1.0
C H:CYS302 4.8 36.2 1.0
O H:CYS323 4.8 36.8 1.0
C H:CYS305 4.9 43.5 1.0
C H:CYS323 4.9 35.0 1.0
HA H:CYS302 4.9 35.9 1.0
H H:SER307 4.9 40.2 1.0
HG12 H:VAL304 4.9 24.6 1.0
N H:LEU306 4.9 44.2 1.0
OG H:SER322 5.0 28.3 1.0

Zinc binding site 8 out of 8 in 6m2c

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Zinc binding site 8 out of 8 in the Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn402

b:26.5
occ:1.00
ND1 H:HIS319 2.2 23.3 1.0
SG H:CYS336 2.3 28.3 1.0
SG H:CYS339 2.4 38.2 1.0
SG H:CYS317 2.5 28.1 1.0
HB2 H:HIS319 2.8 22.6 1.0
HB2 H:CYS317 2.9 30.2 1.0
HB3 H:CYS336 2.9 21.2 1.0
HB2 H:CYS336 2.9 21.2 1.0
CB H:CYS336 2.9 21.2 1.0
CG H:HIS319 3.1 25.9 1.0
CE1 H:HIS319 3.1 25.8 1.0
CB H:CYS317 3.2 30.2 1.0
HE1 H:HIS319 3.3 25.8 1.0
CB H:HIS319 3.4 22.6 1.0
HB3 H:CYS317 3.5 30.2 1.0
H H:CYS339 3.6 26.5 1.0
HB3 H:HIS319 3.8 22.6 1.0
CB H:CYS339 3.9 35.7 1.0
HB H:ILE338 4.0 34.8 1.0
HB3 H:CYS339 4.0 35.7 1.0
H H:HIS319 4.1 26.4 1.0
NE2 H:HIS319 4.2 24.4 1.0
CD2 H:HIS319 4.3 25.0 1.0
N H:CYS339 4.3 26.5 1.0
HD2 H:PHE314 4.3 31.8 1.0
HB2 H:GLN341 4.3 39.0 1.0
H H:GLN341 4.4 30.3 1.0
CA H:CYS336 4.4 27.3 1.0
H H:ILE338 4.5 34.4 1.0
HB2 H:PHE314 4.5 34.2 1.0
CA H:CYS317 4.6 34.0 1.0
HB2 H:CYS339 4.6 35.7 1.0
N H:HIS319 4.6 26.4 1.0
CA H:HIS319 4.6 25.8 1.0
CA H:CYS339 4.6 32.2 1.0
HA H:CYS336 4.8 27.3 1.0
CB H:ILE338 4.9 34.8 1.0
C H:CYS317 4.9 31.7 1.0

Reference:

S.O.Lee, K.S.Ryu, S.-W.Chi. Distinct Mechanism of MUL1-Ring Domain Simultaneously Recruiting E2 Enzyme and the Substrate P53-Tad Domain To Be Published.
Page generated: Thu Aug 21 17:17:49 2025

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