Atomistry » Zinc » PDB 4gy1-4h84 » 4h1q
Atomistry »
  Zinc »
    PDB 4gy1-4h84 »
      4h1q »

Zinc in PDB 4h1q: Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.

Enzymatic activity of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.

All present enzymatic activity of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.:
3.4.24.35;

Protein crystallography data

The structure of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h1q was solved by E.A.Stura, L.Vera, E.Cassar-Lajeunesse, E.Nuti, M.P.Catalani, V.Dive, A.Rossello, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.09 / 1.59
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.140, 48.660, 67.920, 90.00, 102.55, 90.00
R / Rfree (%) 17 / 21.1

Other elements in 4h1q:

The structure of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. also contains other interesting chemical elements:

Calcium (Ca) 7 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. (pdb code 4h1q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h1q:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4h1q

Go back to Zinc Binding Sites List in 4h1q
Zinc binding site 1 out of 4 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.


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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:11.1
occ:1.00
NE2 A:HIS230 2.0 10.7 1.0
NE2 A:HIS236 2.0 9.6 1.0
NE2 A:HIS226 2.1 10.4 1.0
O25 A:0XX307 2.1 17.2 1.0
O23 A:0XX307 2.3 35.3 1.0
C21 A:0XX307 2.9 26.5 1.0
CD2 A:HIS226 3.0 11.2 1.0
CE1 A:HIS230 3.0 11.1 1.0
CE1 A:HIS236 3.0 13.7 1.0
CD2 A:HIS236 3.0 11.0 1.0
N22 A:0XX307 3.0 25.2 1.0
CD2 A:HIS230 3.1 13.6 1.0
CE1 A:HIS226 3.1 10.2 1.0
ND1 A:HIS236 4.1 12.0 1.0
ND1 A:HIS230 4.1 10.2 1.0
CG A:HIS236 4.2 12.0 1.0
CG A:HIS226 4.2 8.6 1.0
ND1 A:HIS226 4.2 8.9 1.0
CG A:HIS230 4.2 11.0 1.0
C20 A:0XX307 4.4 18.4 1.0
N28 A:0XX307 4.4 16.4 1.0
C29 A:0XX307 4.5 20.1 1.0
O17 A:0XX307 4.5 31.4 1.0
C30 A:0XX307 4.5 17.0 1.0
OE1 A:GLN227 4.7 19.5 1.0
CE A:MET244 4.8 7.5 1.0
C2 A:0XX307 5.0 18.8 1.0
N16 A:0XX307 5.0 23.1 1.0

Zinc binding site 2 out of 4 in 4h1q

Go back to Zinc Binding Sites List in 4h1q
Zinc binding site 2 out of 4 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.


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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:15.1
occ:1.00
OD1 A:ASP177 1.9 20.5 1.0
NE2 A:HIS190 1.9 15.4 1.0
NE2 A:HIS175 1.9 13.6 1.0
ND1 A:HIS203 2.0 13.6 1.0
CE1 A:HIS190 2.8 18.3 1.0
CG A:ASP177 2.9 21.6 1.0
CD2 A:HIS175 2.9 15.0 1.0
CE1 A:HIS175 3.0 14.2 1.0
CE1 A:HIS203 3.0 17.8 1.0
CG A:HIS203 3.1 10.5 1.0
CD2 A:HIS190 3.1 12.1 1.0
OD2 A:ASP177 3.1 22.0 1.0
CB A:HIS203 3.4 9.4 1.0
ND1 A:HIS190 3.9 17.5 1.0
ND1 A:HIS175 4.1 14.6 1.0
CG A:HIS175 4.1 15.1 1.0
NE2 A:HIS203 4.1 12.8 1.0
CG A:HIS190 4.1 10.4 1.0
CD2 A:HIS203 4.2 10.2 1.0
CB A:ASP177 4.2 23.1 1.0
O A:TYR179 4.3 17.9 1.0
CE1 A:PHE192 4.4 24.0 1.0
CZ A:PHE181 4.7 14.3 1.0
CE2 A:PHE181 4.7 11.3 1.0
O A:HOH489 4.7 19.9 1.0
CZ A:PHE192 4.8 26.3 1.0
O A:HOH475 4.9 27.4 1.0
CA A:HIS203 4.9 7.3 1.0

Zinc binding site 3 out of 4 in 4h1q

Go back to Zinc Binding Sites List in 4h1q
Zinc binding site 3 out of 4 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.


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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:10.9
occ:1.00
NE2 B:HIS236 2.0 12.7 1.0
NE2 B:HIS230 2.0 7.5 1.0
NE2 B:HIS226 2.1 12.3 1.0
O25 B:0XX306 2.1 14.4 1.0
O23 B:0XX306 2.2 36.3 1.0
C21 B:0XX306 2.7 21.9 1.0
N22 B:0XX306 2.7 20.5 1.0
CD2 B:HIS236 3.0 10.1 1.0
CE1 B:HIS236 3.0 14.6 1.0
CE1 B:HIS230 3.0 10.9 1.0
CD2 B:HIS226 3.0 11.2 1.0
CD2 B:HIS230 3.0 7.5 1.0
CE1 B:HIS226 3.1 11.4 1.0
ND1 B:HIS236 4.1 14.5 1.0
ND1 B:HIS230 4.1 7.1 1.0
CG B:HIS236 4.1 12.5 1.0
CG B:HIS230 4.2 5.7 1.0
ND1 B:HIS226 4.2 7.5 1.0
CG B:HIS226 4.2 8.7 1.0
C20 B:0XX306 4.3 14.0 1.0
C30 B:0XX306 4.5 19.7 1.0
O17 B:0XX306 4.5 29.8 1.0
C29 B:0XX306 4.5 24.3 1.0
N28 B:0XX306 4.6 24.4 1.0
OE1 B:GLN227 4.7 18.7 1.0
CE B:MET244 4.9 8.6 1.0
N16 B:0XX306 4.9 18.7 1.0
C3 B:0XX306 4.9 17.4 1.0
C2 B:0XX306 5.0 14.1 1.0

Zinc binding site 4 out of 4 in 4h1q

Go back to Zinc Binding Sites List in 4h1q
Zinc binding site 4 out of 4 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.


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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:13.8
occ:1.00
OD1 B:ASP177 1.9 16.8 1.0
NE2 B:HIS175 2.0 11.1 1.0
NE2 B:HIS190 2.0 14.1 1.0
ND1 B:HIS203 2.1 10.4 1.0
CG B:ASP177 2.8 23.6 1.0
CE1 B:HIS190 2.9 14.3 1.0
CD2 B:HIS175 3.0 16.1 1.0
CE1 B:HIS175 3.0 16.0 1.0
CE1 B:HIS203 3.0 13.4 1.0
CD2 B:HIS190 3.1 13.5 1.0
CG B:HIS203 3.1 13.6 1.0
OD2 B:ASP177 3.2 23.9 1.0
CB B:HIS203 3.5 9.1 1.0
ND1 B:HIS190 4.1 15.7 1.0
ND1 B:HIS175 4.1 14.4 1.0
CG B:HIS175 4.1 19.2 1.0
O B:TYR179 4.1 22.0 1.0
CB B:ASP177 4.2 20.6 1.0
NE2 B:HIS203 4.2 12.1 1.0
CG B:HIS190 4.2 15.3 1.0
CD2 B:HIS203 4.2 10.1 1.0
CE1 B:PHE192 4.5 18.2 1.0
CZ B:PHE181 4.6 10.1 1.0
CE2 B:PHE181 4.8 11.7 1.0
O B:HOH466 4.8 25.4 1.0
O B:HOH477 4.9 25.4 1.0
CZ B:PHE192 4.9 15.7 1.0
CA B:HIS203 5.0 8.9 1.0

Reference:

C.Antoni, L.Vera, L.Devel, M.P.Catalani, B.Czarny, E.Cassar-Lajeunesse, E.Nuti, A.Rossello, V.Dive, E.A.Stura. Crystallization of Bi-Functional Ligand Protein Complexes. J.Struct.Biol. V. 182 246 2013.
ISSN: ISSN 1047-8477
PubMed: 23567804
DOI: 10.1016/J.JSB.2013.03.015
Page generated: Wed Dec 16 05:21:24 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy