Atomistry » Calcium » PDB 1m9i-1mr8 » 1mmb
Atomistry »
  Calcium »
    PDB 1m9i-1mr8 »
      1mmb »

Calcium in PDB 1mmb: Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8

Enzymatic activity of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8

All present enzymatic activity of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8:
3.4.24.34;

Protein crystallography data

The structure of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8, PDB code: 1mmb was solved by W.Bode, F.Grams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.670, 69.640, 73.400, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / n/a

Other elements in 1mmb:

The structure of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8 (pdb code 1mmb). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8, PDB code: 1mmb:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1mmb

Go back to Calcium Binding Sites List in 1mmb
Calcium binding site 1 out of 2 in the Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca996

b:16.1
occ:1.00
H2 A:HOH1027 1.7 15.0 1.0
H1 A:HOH1026 1.7 15.0 1.0
O A:HOH1027 2.2 22.3 1.0
O A:ASP137 2.3 18.7 1.0
O A:GLY169 2.3 25.9 1.0
O A:GLY171 2.3 15.3 1.0
OD2 A:ASP173 2.3 13.0 1.0
H1 A:HOH1027 2.4 15.0 1.0
O A:HOH1026 2.5 17.3 1.0
H2 A:HOH1026 2.5 15.0 1.0
CG A:ASP173 3.3 14.9 1.0
C A:ASP137 3.4 19.6 1.0
C A:GLY169 3.5 25.3 1.0
HD22 A:ASN139 3.5 15.0 1.0
C A:GLY171 3.5 16.3 1.0
OD1 A:ASP173 3.7 14.0 1.0
H A:ASP173 3.8 15.0 1.0
H A:ASN139 3.9 15.0 1.0
C A:ILE170 3.9 20.9 1.0
N A:GLY171 4.0 19.4 1.0
H2 A:HOH1028 4.0 15.0 1.0
O A:ILE170 4.1 22.6 1.0
H1 A:HOH1168 4.1 15.0 1.0
N A:ASP173 4.2 12.0 1.0
O A:GLY167 4.2 23.9 1.0
H1 A:HOH1167 4.2 15.0 1.0
H A:GLY171 4.3 15.0 1.0
CA A:ASP137 4.3 20.8 1.0
CA A:GLY171 4.3 16.7 1.0
N A:ILE170 4.3 24.2 1.0
O A:ALA136 4.4 21.2 1.0
H2 A:HOH1045 4.4 15.0 1.0
ND2 A:ASN139 4.4 17.0 1.0
N A:ILE138 4.4 17.6 1.0
CA A:ILE170 4.4 22.6 1.0
CA A:GLY169 4.4 25.3 1.0
N A:GLY172 4.5 14.9 1.0
CA A:ILE138 4.5 16.2 1.0
N A:GLY169 4.5 25.5 1.0
CB A:ASP173 4.6 12.8 1.0
C A:GLY172 4.6 12.2 1.0
H A:GLY169 4.6 15.0 1.0
CA A:GLY172 4.6 12.4 1.0
HD21 A:ASN139 4.7 15.0 1.0
N A:ASN139 4.7 13.7 1.0
CA A:ASP173 4.8 12.0 1.0
O A:HOH1045 4.9 26.2 1.0
C A:GLN168 4.9 26.6 1.0
H2 A:HOH1168 4.9 15.0 1.0

Calcium binding site 2 out of 2 in 1mmb

Go back to Calcium Binding Sites List in 1mmb
Calcium binding site 2 out of 2 in the Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex of BB94 with the Catalytic Domain of Matrix Metalloproteinase-8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca997

b:12.7
occ:1.00
OE1 A:GLU180 2.1 14.7 1.0
OD2 A:ASP154 2.3 17.2 1.0
O A:GLY155 2.3 18.2 1.0
O A:ILE159 2.3 18.8 1.0
OD1 A:ASP177 2.4 13.8 1.0
O A:ASN157 2.5 17.7 1.0
CD A:GLU180 3.4 15.9 1.0
H A:ASP154 3.4 15.0 1.0
CG A:ASP177 3.4 15.7 1.0
C A:ILE159 3.5 18.6 1.0
CG A:ASP154 3.5 19.1 1.0
C A:GLY155 3.5 16.8 1.0
C A:ASN157 3.6 16.4 1.0
H A:ILE159 3.9 15.0 1.0
H A:GLY155 3.9 15.0 1.0
N A:ILE159 3.9 17.0 1.0
N A:GLY155 4.0 18.2 1.0
N A:ASN157 4.0 17.1 1.0
CB A:ASP177 4.0 14.9 1.0
C A:PRO156 4.1 17.0 1.0
OE2 A:GLU180 4.1 15.6 1.0
H A:ASN157 4.1 15.0 1.0
OD1 A:ASP154 4.1 18.1 1.0
C A:ASP154 4.2 18.8 1.0
N A:ASP154 4.2 19.2 1.0
C A:GLY158 4.2 16.9 1.0
CA A:ILE159 4.3 19.0 1.0
OD2 A:ASP177 4.3 13.9 1.0
CA A:GLY155 4.4 16.9 1.0
CA A:ASN157 4.4 17.2 1.0
O A:PRO156 4.4 16.2 1.0
N A:LEU160 4.4 17.6 1.0
CG A:GLU180 4.4 16.9 1.0
N A:PRO156 4.5 16.3 1.0
CA A:PRO156 4.5 16.5 1.0
CA A:ASP154 4.5 18.6 1.0
N A:GLY158 4.6 15.7 1.0
CB A:ASP154 4.6 18.5 1.0
CA A:LEU160 4.7 16.1 1.0
CA A:GLY158 4.7 15.3 1.0
O A:ASP154 4.7 18.3 1.0
O A:GLY158 4.8 17.2 1.0
CG1 A:ILE159 4.9 23.5 1.0
H1 A:HOH1021 4.9 15.0 1.0

Reference:

F.Grams, M.Crimmin, L.Hinnes, P.Huxley, M.Pieper, H.Tschesche, W.Bode. Structure Determination and Analysis of Human Neutrophil Collagenase Complexed with A Hydroxamate Inhibitor. Biochemistry V. 34 14012 1995.
ISSN: ISSN 0006-2960
PubMed: 7577999
DOI: 10.1021/BI00043A007
Page generated: Sat Dec 12 03:07:05 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy