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Zinc in PDB 2y6i: Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution

Enzymatic activity of Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution

All present enzymatic activity of Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution, PDB code: 2y6i was solved by U.Eckhard, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 93.28 / 3.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.120, 108.840, 181.030, 90.00, 90.00, 90.00
R / Rfree (%) 21.64 / 26.633

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution (pdb code 2y6i). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution, PDB code: 2y6i:

Zinc binding site 1 out of 1 in 2y6i

Go back to Zinc Binding Sites List in 2y6i
Zinc binding site 1 out of 1 in the Crystal Structure of Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution


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 Collagenase G From Clostridium Histolyticum in Complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1791

b:55.6
occ:1.00
 O A:HOH2042 2.1 58.3 1.0
O2 B:IPI1 2.1 72.1 1.0
NE2 A:HIS523 2.1 63.0 1.0
OE1 A:GLU555 2.1 85.0 1.0
NE2 A:HIS527 2.1 60.4 1.0
OE2 A:GLU555 2.7 83.3 1.0
CD A:GLU555 2.7 82.5 1.0
CD2 A:HIS523 3.0 59.4 1.0
CE1 A:HIS527 3.0 56.7 1.0
CD2 A:HIS527 3.1 56.1 1.0
CE1 A:HIS523 3.2 61.4 1.0
P B:IPI1 3.4 79.4 1.0
N B:GLY2 3.9 80.4 1.0
O1 B:IPI1 4.0 78.6 1.0
CG A:HIS523 4.1 58.1 1.0
ND1 A:HIS527 4.2 55.2 1.0
OE2 A:GLU524 4.2 57.3 1.0
CG A:GLU555 4.2 75.7 1.0
ND1 A:HIS523 4.2 60.5 1.0
CG A:HIS527 4.2 53.9 1.0
CB A:ALA558 4.4 57.2 1.0
CA A:GLU555 4.5 66.1 1.0
CB A:GLU555 4.7 69.6 1.0
O A:HOH2033 4.8 57.0 1.0
C5 B:IPI1 4.8 78.7 1.0
CD A:GLU524 4.9 56.1 1.0
C3 B:IPI1 4.9 79.3 1.0
OE1 A:GLU524 5.0 55.8 1.0

Reference:

U.Eckhard, E.Schoenauer, D.Nuess, H.Brandstetter. Structure of Collagenase G Reveals A Chew-and -Digest Mechanism of Bacterial Collagenolysis Nat.Struct.Mol.Biol. V. 18 1109 2011.
ISSN: ISSN 1545-9993
PubMed: 21947205
DOI: 10.1038/NSMB.2127
Page generated: Thu Oct 17 05:45:00 2024

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