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Zinc in PDB 4zd5: Catalytic Domain of SST2 F403A Mutant

Protein crystallography data

The structure of Catalytic Domain of SST2 F403A Mutant, PDB code: 4zd5 was solved by R.K.Shrestha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.49 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.646, 74.898, 64.587, 90.00, 112.91, 90.00
R / Rfree (%) 20 / 24.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of SST2 F403A Mutant (pdb code 4zd5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Catalytic Domain of SST2 F403A Mutant, PDB code: 4zd5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4zd5

Go back to Zinc Binding Sites List in 4zd5
Zinc binding site 1 out of 4 in the Catalytic Domain of SST2 F403A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Domain of SST2 F403A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:24.6
occ:1.00
OD2 A:ASP354 1.9 18.7 1.0
O A:HOH608 2.0 23.8 1.0
NE2 A:HIS341 2.0 18.1 1.0
NE2 A:HIS343 2.1 27.2 1.0
CG A:ASP354 2.6 20.1 1.0
OD1 A:ASP354 2.7 16.0 1.0
CE1 A:HIS341 2.9 19.2 1.0
CD2 A:HIS343 3.0 26.2 1.0
CD2 A:HIS341 3.1 18.4 1.0
CE1 A:HIS343 3.2 29.0 1.0
OE2 A:GLU286 3.9 25.6 1.0
OG A:SER351 4.0 30.4 1.0
ND1 A:HIS341 4.0 20.6 1.0
CB A:ASP354 4.1 20.5 1.0
CG A:HIS343 4.2 28.7 1.0
CG A:HIS341 4.2 19.7 1.0
C1 A:EDO505 4.2 30.2 1.0
O1 A:EDO505 4.2 33.5 1.0
ND1 A:HIS343 4.2 28.3 1.0
CB A:SER351 4.4 28.0 1.0
O A:PHE349 4.4 29.0 1.0
N A:SER351 4.4 26.3 1.0
OE1 A:GLU286 4.5 24.8 1.0
CD A:GLU286 4.5 25.3 1.0
CG1 A:VAL372 4.7 25.2 1.0

Zinc binding site 2 out of 4 in 4zd5

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Zinc binding site 2 out of 4 in the Catalytic Domain of SST2 F403A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Domain of SST2 F403A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:32.5
occ:1.00
NE2 A:HIS404 1.9 36.9 1.0
NE2 A:HIS406 2.0 30.4 1.0
NE2 A:HIS356 2.1 29.9 1.0
SG A:CYS397 2.4 33.0 1.0
CE1 A:HIS406 2.6 33.9 1.0
CD2 A:HIS404 2.9 35.2 1.0
CE1 A:HIS404 2.9 36.5 1.0
CE1 A:HIS356 3.0 29.3 1.0
CD2 A:HIS356 3.1 29.7 1.0
CD2 A:HIS406 3.2 37.8 1.0
CB A:CYS397 3.4 36.2 1.0
ND1 A:HIS406 3.8 36.3 1.0
CG A:HIS404 4.0 39.8 1.0
ND1 A:HIS404 4.0 35.8 1.0
CG A:HIS406 4.1 37.2 1.0
ND1 A:HIS356 4.1 30.1 1.0
CG A:HIS356 4.2 29.7 1.0
OG A:SER352 4.2 38.2 1.0
CD1 A:ILE394 4.7 28.6 1.0
CA A:CYS397 4.7 34.9 1.0
O A:CYS397 4.9 37.0 1.0
C A:CYS397 4.9 37.5 1.0

Zinc binding site 3 out of 4 in 4zd5

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Zinc binding site 3 out of 4 in the Catalytic Domain of SST2 F403A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Catalytic Domain of SST2 F403A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:31.1
occ:1.00
CE1 B:HIS404 2.0 35.2 1.0
NE2 B:HIS406 2.0 30.4 1.0
NE2 B:HIS356 2.1 27.1 1.0
SG B:CYS397 2.3 30.2 1.0
CE1 B:HIS406 2.7 32.9 1.0
NE2 B:HIS404 2.8 38.1 1.0
CD2 B:HIS356 3.1 25.4 1.0
CE1 B:HIS356 3.1 26.6 1.0
ND1 B:HIS404 3.1 43.2 1.0
CD2 B:HIS406 3.2 34.2 1.0
CB B:CYS397 3.3 34.3 1.0
ND1 B:HIS406 3.9 31.8 1.0
CD2 B:HIS404 4.0 41.0 1.0
ND1 B:HIS356 4.2 25.0 1.0
CG B:HIS406 4.2 33.2 1.0
CG B:HIS404 4.2 39.5 1.0
CG B:HIS356 4.2 24.5 1.0
OG B:SER352 4.3 35.1 1.0
CD1 B:ILE394 4.6 29.6 1.0
CA B:CYS397 4.7 36.5 1.0
O B:CYS397 4.9 41.0 1.0
C B:CYS397 4.9 40.5 1.0
NH2 A:ARG398 4.9 70.8 1.0

Zinc binding site 4 out of 4 in 4zd5

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Zinc binding site 4 out of 4 in the Catalytic Domain of SST2 F403A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Catalytic Domain of SST2 F403A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:23.9
occ:1.00
O B:HOH603 1.8 20.3 1.0
OD2 B:ASP354 1.9 17.8 1.0
NE2 B:HIS341 2.1 21.3 1.0
NE2 B:HIS343 2.1 22.0 1.0
CG B:ASP354 2.5 18.2 1.0
OD1 B:ASP354 2.6 14.8 1.0
CD2 B:HIS343 2.9 19.5 1.0
CE1 B:HIS341 3.1 19.7 1.0
CD2 B:HIS341 3.1 23.1 1.0
CE1 B:HIS343 3.2 22.9 1.0
OE2 B:GLU286 3.8 26.1 1.0
OG B:SER351 3.8 28.3 1.0
CB B:ASP354 4.0 20.0 1.0
CG B:HIS343 4.1 22.2 1.0
ND1 B:HIS341 4.2 21.4 1.0
CG B:HIS341 4.2 22.2 1.0
ND1 B:HIS343 4.2 23.2 1.0
CB B:SER351 4.3 27.7 1.0
O B:PHE349 4.5 25.8 1.0
N B:SER351 4.5 25.8 1.0
CD B:GLU286 4.6 25.6 1.0
OE1 B:GLU286 4.7 22.6 1.0
CG1 B:VAL372 4.9 22.9 1.0
O B:THR342 5.0 24.6 1.0

Reference:

R.K.Shrestha, R.K.Shrestha. N/A N/A.
Page generated: Sun Oct 27 11:41:39 2024

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