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Chlorine in PDB 1ck7: Gelatinase A (Full-Length)

Enzymatic activity of Gelatinase A (Full-Length)

All present enzymatic activity of Gelatinase A (Full-Length):
3.4.24.24;

Protein crystallography data

The structure of Gelatinase A (Full-Length), PDB code: 1ck7 was solved by E.Morgunova, A.Tuuttila, U.Bergmann, M.Isupov, Y.Lindqvist, G.Schneider, K.Tryggvason, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 2.80
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 121.320, 121.320, 345.110, 90.00, 90.00, 90.00
R / Rfree (%) 28.6 / 32.7

Other elements in 1ck7:

The structure of Gelatinase A (Full-Length) also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Calcium (Ca) 3 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Gelatinase A (Full-Length) (pdb code 1ck7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Gelatinase A (Full-Length), PDB code: 1ck7:

Chlorine binding site 1 out of 1 in 1ck7

Go back to Chlorine Binding Sites List in 1ck7
Chlorine binding site 1 out of 1 in the Gelatinase A (Full-Length)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Gelatinase A (Full-Length) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl995

b:58.6
occ:1.00
NA A:NA996 3.1 61.1 1.0
CB A:ALA522 3.6 53.2 1.0
N A:ALA571 3.6 67.7 1.0
N A:VAL523 3.6 56.6 1.0
CA A:ALA522 3.7 51.9 1.0
O A:ALA571 3.8 76.5 1.0
O A:VAL523 3.9 73.2 1.0
O A:ASP618 4.0 0.7 1.0
CA A:GLY477 4.0 58.0 1.0
O A:ILE478 4.0 68.3 1.0
CB A:ALA619 4.1 0.3 1.0
N A:ILE478 4.1 60.6 1.0
CA A:ALA570 4.1 64.3 1.0
CA A:ALA619 4.1 0.5 1.0
C A:ALA570 4.2 65.8 1.0
C A:ALA522 4.2 53.6 1.0
N A:VAL620 4.3 0.4 1.0
CB A:ALA571 4.4 71.7 1.0
CA A:ALA571 4.4 71.1 1.0
C A:ALA571 4.5 75.6 1.0
O A:ASP569 4.6 68.5 1.0
C A:GLY477 4.6 59.5 1.0
CA A:VAL523 4.6 64.4 1.0
O A:ASP521 4.7 52.3 1.0
C A:VAL523 4.7 69.9 1.0
CA A:CA994 4.7 63.8 1.0
O A:VAL620 4.8 0.7 1.0
C A:ALA619 4.8 0.3 1.0
O A:ASP476 4.9 59.2 1.0
N A:ALA522 5.0 50.1 1.0
C A:ILE478 5.0 67.5 1.0
CB A:ALA570 5.0 76.5 1.0

Reference:

E.Morgunova, A.Tuuttila, U.Bergmann, M.Isupov, Y.Lindqvist, G.Schneider, K.Tryggvason. Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed. Science V. 284 1667 1999.
ISSN: ISSN 0036-8075
PubMed: 10356396
DOI: 10.1126/SCIENCE.284.5420.1667
Page generated: Sat Dec 12 08:33:03 2020

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