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Zinc in PDB 1r7o: Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa

Enzymatic activity of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa

All present enzymatic activity of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa:
3.2.1.78;

Protein crystallography data

The structure of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa, PDB code: 1r7o was solved by A.J.Oakley, M.C.J.Wilce, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.29 / 1.85
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 93.240, 93.240, 54.830, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 17

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa (pdb code 1r7o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa, PDB code: 1r7o:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 1r7o

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Zinc binding site 1 out of 5 in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:16.0
occ:1.00
NE2 A:HIS71 2.1 13.1 1.0
OE2 A:GLU67 2.1 18.8 1.0
O A:HOH2270 2.1 26.7 1.0
O A:HOH2108 2.3 18.0 1.0
CD2 A:HIS71 3.0 12.4 1.0
CE1 A:HIS71 3.0 13.3 1.0
CD A:GLU67 3.1 19.6 1.0
OE1 A:GLU67 3.4 20.9 1.0
O A:HOH2351 4.1 41.6 1.0
O A:HOH2089 4.1 12.2 1.0
ND1 A:HIS71 4.2 13.4 1.0
CG A:HIS71 4.2 12.2 1.0
O A:GLU67 4.3 15.5 1.0
CG A:GLU67 4.4 18.0 1.0
O A:HOH2191 4.7 32.6 1.0

Zinc binding site 2 out of 5 in 1r7o

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Zinc binding site 2 out of 5 in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1002

b:23.4
occ:1.00
O A:HOH2121 2.1 18.5 1.0
OD2 A:ASP222 2.1 15.2 1.0
O A:HOH2196 2.1 22.3 1.0
O A:HOH2192 2.1 19.4 1.0
O A:HOH2329 2.3 25.6 1.0
O A:HOH2218 2.3 21.7 1.0
CG A:ASP222 3.0 14.4 1.0
OD1 A:ASP222 3.2 14.6 1.0
O A:THR214 4.0 13.8 1.0
NZ A:LYS223 4.1 24.2 1.0
O A:HOH2426 4.1 39.3 1.0
O A:HOH2234 4.3 27.4 1.0
O A:HOH2115 4.4 17.2 1.0
CB A:ASP222 4.5 14.2 1.0
O A:HOH2284 4.5 33.8 1.0
O A:HOH2135 4.9 21.4 1.0

Zinc binding site 3 out of 5 in 1r7o

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Zinc binding site 3 out of 5 in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1003

b:19.8
occ:1.00
OD2 A:ASP111 1.9 13.0 1.0
O A:HOH2501 1.9 22.1 1.0
OE2 A:GLU121 2.0 24.7 1.0
NE2 A:HIS79 2.1 19.5 1.0
OE1 A:GLU121 2.4 24.5 1.0
CD A:GLU121 2.5 20.2 1.0
CG A:ASP111 2.9 11.8 1.0
CE1 A:HIS79 3.0 19.2 1.0
OD1 A:ASP111 3.1 12.2 1.0
CD2 A:HIS79 3.2 18.4 1.0
O A:HOH2024 3.8 11.7 1.0
O A:HOH2516 3.9 49.5 1.0
CG A:GLU121 4.0 19.4 1.0
ND1 A:HIS79 4.2 17.6 1.0
CB A:ASP111 4.3 10.8 1.0
CG A:HIS79 4.3 17.4 1.0
NE2 A:GLN78 4.3 12.6 1.0
CZ2 A:TRP360 4.5 23.1 1.0
O A:HOH2398 4.5 34.1 1.0
CD1 A:LEU113 4.7 15.9 1.0
CH2 A:TRP360 4.8 21.9 1.0
OE1 A:GLN83 4.8 29.5 1.0
N A:ASP111 4.8 10.4 1.0
CG A:GLN78 4.9 14.4 1.0
CD2 A:HIS143 4.9 12.8 0.3
CB A:GLU121 4.9 17.2 1.0
CB A:LEU113 5.0 11.8 1.0

Zinc binding site 4 out of 5 in 1r7o

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Zinc binding site 4 out of 5 in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1004

b:15.8
occ:0.67
ZN A:ZN1004 0.0 15.8 0.7
OD1 A:ASP283 1.8 19.2 1.0
ZN A:ZN1004 1.9 11.9 0.3
OE2 A:GLU320 1.9 17.2 1.0
NH1 A:ARG208 2.2 13.1 1.0
ND1 A:HIS211 2.2 15.4 1.0
CD A:GLU320 2.6 16.8 1.0
CG A:ASP283 2.6 16.6 1.0
OD2 A:ASP283 2.8 21.1 1.0
CZ A:ARG208 3.1 13.4 1.0
CG A:HIS211 3.1 11.7 1.0
CE1 A:HIS211 3.2 14.4 1.0
CG A:GLU320 3.2 16.2 1.0
NH2 A:ARG208 3.2 15.4 1.0
CB A:HIS211 3.3 11.1 1.0
OE1 A:GLU320 3.4 23.4 1.0
OE2 A:GLU212 3.8 14.5 1.0
CB A:GLU320 3.9 14.0 1.0
CB A:ASP283 4.0 14.2 1.0
OG A:SER255 4.1 10.5 0.7
CD2 A:HIS211 4.2 14.3 1.0
OG A:SER255 4.2 9.6 0.3
CG A:GLU212 4.3 11.8 1.0
NE2 A:HIS211 4.3 14.5 1.0
NE A:ARG208 4.3 12.2 1.0
CD A:GLU212 4.4 12.8 1.0
CA A:HIS211 4.8 10.7 1.0
CD A:ARG208 5.0 11.8 1.0
CB A:SER255 5.0 10.1 0.3

Zinc binding site 5 out of 5 in 1r7o

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Zinc binding site 5 out of 5 in the Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Apo-Mannanase 26A From Psudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1004

b:11.9
occ:0.33
ZN A:ZN1004 0.0 11.9 0.3
OD1 A:ASP283 1.7 19.2 1.0
ZN A:ZN1004 1.9 15.8 0.7
ND1 A:HIS211 1.9 15.4 1.0
OE2 A:GLU212 2.0 14.5 1.0
CE1 A:HIS211 2.5 14.4 1.0
OE2 A:GLU320 2.6 17.2 1.0
CD A:GLU212 2.6 12.8 1.0
CG A:GLU212 2.8 11.8 1.0
CG A:ASP283 2.9 16.6 1.0
CD A:GLU320 2.9 16.8 1.0
OE1 A:GLU320 3.0 23.4 1.0
CG A:HIS211 3.1 11.7 1.0
OE1 A:GLU212 3.7 14.8 1.0
NE2 A:HIS211 3.7 14.5 1.0
CB A:ASP283 3.7 14.2 1.0
OD2 A:ASP283 3.8 21.1 1.0
CB A:HIS211 3.8 11.1 1.0
CD2 A:HIS211 4.0 14.3 1.0
NH1 A:ARG208 4.0 13.1 1.0
CG A:GLU320 4.1 16.2 1.0
CB A:GLU212 4.2 11.3 1.0
O A:HOH2229 4.2 32.8 1.0
O A:HOH2380 4.4 35.7 1.0
CB A:GLU320 4.4 14.0 1.0
N A:GLU212 4.6 11.0 1.0
C A:HIS211 4.8 10.8 1.0
NH2 A:ARG208 4.9 15.4 1.0
CZ A:ARG208 4.9 13.4 1.0
CA A:HIS211 5.0 10.7 1.0
CA A:GLU212 5.0 11.3 1.0

Reference:

A.J.Oakley, M.C.J.Wilce. Structural Investigation of Mannanase 26A From Pseudomonas Cellulosa Reveals An Induced Fit Mechanism and A Non-Substrate Ligand Binding Site To Be Published.
Page generated: Wed Dec 16 03:02:35 2020

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