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Zinc in PDB 3ba0: Crystal Structure of Full-Length Human Mmp-12

Enzymatic activity of Crystal Structure of Full-Length Human Mmp-12

All present enzymatic activity of Crystal Structure of Full-Length Human Mmp-12:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of Full-Length Human Mmp-12, PDB code: 3ba0 was solved by I.Bertini, V.Calderone, M.Fragai, R.Jaiswal, C.Luchinat, M.Melikian, E.Myonas, D.I.Svergun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.70 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 135.037, 60.148, 59.611, 90.00, 90.74, 90.00
R / Rfree (%) 23.6 / 31.9

Other elements in 3ba0:

The structure of Crystal Structure of Full-Length Human Mmp-12 also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Full-Length Human Mmp-12 (pdb code 3ba0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Full-Length Human Mmp-12, PDB code: 3ba0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3ba0

Go back to Zinc Binding Sites List in 3ba0
Zinc binding site 1 out of 2 in the Crystal Structure of Full-Length Human Mmp-12


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 Full-Length Human Mmp-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn471

b:11.5
occ:1.00
NE2 A:HIS222 2.3 18.9 1.0
O2 A:HAE477 2.5 17.1 1.0
NE2 A:HIS228 2.6 21.6 1.0
O A:HAE477 2.9 15.4 1.0
OE1 A:GLU219 3.1 19.6 1.0
CE1 A:HIS222 3.2 10.6 1.0
CD2 A:HIS222 3.2 20.9 1.0
NE2 A:HIS218 3.3 4.3 1.0
CD2 A:HIS228 3.4 15.4 1.0
C2 A:HAE477 3.4 16.1 1.0
CE1 A:HIS228 3.5 20.2 1.0
N A:HAE477 3.6 14.3 1.0
CD2 A:HIS218 3.8 2.0 1.0
OE2 A:GLU219 3.8 24.3 1.0
CD A:GLU219 3.8 24.8 1.0
CE1 A:HIS218 4.0 7.0 1.0
ND1 A:HIS222 4.1 15.9 1.0
CG A:HIS222 4.2 13.5 1.0
ND1 A:HIS228 4.6 22.2 1.0
CG A:HIS228 4.6 18.2 1.0
CG A:HIS218 4.7 2.0 1.0
ND1 A:HIS218 4.8 2.0 1.0
CG A:PRO238 4.9 19.2 1.0
C1 A:HAE477 4.9 9.1 1.0

Zinc binding site 2 out of 2 in 3ba0

Go back to Zinc Binding Sites List in 3ba0
Zinc binding site 2 out of 2 in the Crystal Structure of Full-Length Human Mmp-12


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 Full-Length Human Mmp-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn472

b:2.0
occ:1.00
NE2 A:HIS168 1.8 2.0 1.0
NE2 A:HIS183 2.0 6.4 1.0
OD1 A:ASP170 2.2 15.0 1.0
ND1 A:HIS196 2.3 2.0 1.0
CE1 A:HIS183 2.6 9.8 1.0
CD2 A:HIS168 2.7 2.0 1.0
CG A:ASP170 2.8 15.0 1.0
CE1 A:HIS168 2.9 2.0 1.0
OD2 A:ASP170 2.9 15.0 1.0
CE1 A:HIS196 3.2 2.0 1.0
CD2 A:HIS183 3.2 5.6 1.0
CG A:HIS196 3.4 2.0 1.0
CB A:HIS196 3.8 2.0 1.0
ND1 A:HIS183 3.9 6.8 1.0
CB A:ASP170 3.9 15.0 1.0
CG A:HIS168 3.9 2.0 1.0
ND1 A:HIS168 3.9 2.0 1.0
CG A:HIS183 4.2 2.0 1.0
CE2 A:PHE185 4.2 2.0 1.0
NE2 A:HIS196 4.3 2.0 1.0
CD2 A:HIS196 4.5 2.0 1.0
O A:HIS172 4.6 4.8 1.0
CZ A:PHE185 4.6 6.8 1.0

Reference:

I.Bertini, V.Calderone, M.Fragai, R.Jaiswal, C.Luchinat, M.Melikian, E.Mylonas, D.I.Svergun. Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length Mmp-12. J.Am.Chem.Soc. V. 130 7011 2008.
ISSN: ISSN 0002-7863
PubMed: 18465858
DOI: 10.1021/JA710491Y
Page generated: Thu Oct 24 11:28:22 2024

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