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Calcium in PDB 1rtg: C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2

Enzymatic activity of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2

All present enzymatic activity of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2:
3.4.24.24;

Protein crystallography data

The structure of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2, PDB code: 1rtg was solved by U.Gohlke, W.Bode, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.780, 58.850, 93.140, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / n/a

Other elements in 1rtg:

The structure of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2 (pdb code 1rtg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2, PDB code: 1rtg:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1rtg

Go back to Calcium Binding Sites List in 1rtg
Calcium binding site 1 out of 2 in the C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2

b:14.8
occ:1.00
O A:HOH33 2.4 24.9 1.0
O A:VAL523 2.6 14.8 1.0
O A:ALA571 2.6 21.0 1.0
O A:ILE478 2.7 4.2 1.0
O A:VAL620 2.7 13.7 1.0
CL A:CL1 3.1 30.6 1.0
C A:VAL523 3.8 8.5 1.0
C A:ALA571 3.9 12.8 1.0
C A:ILE478 3.9 5.9 1.0
C A:VAL620 3.9 16.1 1.0
CB A:ALA479 4.0 3.6 1.0
CA A:ALA479 4.3 8.1 1.0
CB A:TYR524 4.3 7.8 1.0
CA A:TYR524 4.3 12.8 1.0
N A:VAL620 4.4 15.9 1.0
CB A:PHE572 4.4 9.4 1.0
N A:TYR524 4.5 9.9 1.0
N A:ALA479 4.5 13.6 1.0
CA A:PHE572 4.6 9.6 1.0
N A:ALA571 4.6 6.9 1.0
N A:PHE572 4.7 12.6 1.0
CA A:VAL620 4.8 15.1 1.0
N A:VAL621 4.8 15.6 1.0
N A:VAL523 4.8 5.0 1.0
CA A:ALA571 4.8 6.8 1.0
CA A:VAL621 4.9 16.5 1.0
N A:ILE478 4.9 6.4 1.0
CA A:VAL523 4.9 8.1 1.0
CB A:VAL621 4.9 17.3 1.0
CG1 A:VAL620 5.0 13.5 1.0

Calcium binding site 2 out of 2 in 1rtg

Go back to Calcium Binding Sites List in 1rtg
Calcium binding site 2 out of 2 in the C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of C-Terminal Domain (Haemopexin-Like Domain) of Human Matrix Metalloproteinase-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca5

b:20.0
occ:1.00
O A:ASP618 2.4 14.0 1.0
O A:ASP476 2.5 18.6 1.0
O A:ASP521 2.5 6.5 1.0
O A:ASP569 2.5 8.7 1.0
O A:HOH28 2.9 20.1 1.0
C A:ASP618 3.5 9.8 1.0
C A:ASP476 3.5 8.4 1.0
C A:ASP569 3.7 7.2 1.0
C A:ASP521 3.7 6.2 1.0
O A:HOH85 3.8 55.8 1.0
CA A:ASP618 4.1 10.8 1.0
N A:GLY477 4.4 8.0 1.0
CA A:ASP476 4.4 5.4 1.0
CA A:GLY477 4.4 8.3 1.0
CA A:ASP569 4.5 5.5 1.0
N A:ALA619 4.5 4.8 1.0
CA A:ASP521 4.6 8.4 1.0
O A:HOH43 4.6 26.8 1.0
N A:ALA522 4.7 2.0 1.0
CA A:ALA522 4.7 4.1 1.0
N A:ALA570 4.7 5.7 1.0
O A:PHE475 4.8 11.7 1.0
CL A:CL1 4.8 30.6 1.0
O A:LEU617 4.8 11.3 1.0
CB A:ALA522 4.8 7.5 1.0
CA A:ALA570 4.8 3.6 1.0
CA A:ALA619 4.8 8.0 1.0
O A:HOH70 4.9 53.5 1.0
CB A:ASP618 4.9 17.2 1.0

Reference:

U.Gohlke, F.X.Gomis-Ruth, T.Crabbe, G.Murphy, A.J.Docherty, W.Bode. The C-Terminal (Haemopexin-Like) Domain Structure of Human Gelatinase A (MMP2): Structural Implications For Its Function. Febs Lett. V. 378 126 1996.
ISSN: ISSN 0014-5793
PubMed: 8549817
DOI: 10.1016/0014-5793(95)01435-7
Page generated: Thu Jul 11 22:17:27 2024

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