Zinc in PDB 7z5u: Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor

Enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor

All present enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor, PDB code: 7z5u was solved by E.Schoenauer, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.46 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.306, 78.385, 96.411, 90, 90, 90
R / Rfree (%) 18 / 20.7

Other elements in 7z5u:

The structure of Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor (pdb code 7z5u). 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 the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor, PDB code: 7z5u:

Zinc binding site 1 out of 1 in 7z5u

Go back to Zinc Binding Sites List in 7z5u
Zinc binding site 1 out of 1 in the Crystal Structure of the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor


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 the Peptidase Domain of Collagenase G From Clostridium Histolyticum in Complex with A Hydroxamate-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:20.0
occ:1.00
OE1 A:GLU555 2.1 16.7 1.0
NE2 A:HIS527 2.1 18.9 1.0
O3 A:IFW802 2.1 19.3 1.0
NE2 A:HIS523 2.2 18.0 1.0
O4 A:IFW802 2.2 22.9 1.0
H27 A:IFW802 2.3 27.5 1.0
C19 A:IFW802 2.8 23.1 1.0
CD A:GLU555 2.8 17.7 1.0
N3 A:IFW802 2.9 22.0 1.0
OE2 A:GLU555 3.0 18.4 1.0
CD2 A:HIS523 3.0 19.0 1.0
CD2 A:HIS527 3.0 20.6 1.0
CE1 A:HIS527 3.1 16.4 1.0
HD2 A:HIS523 3.1 22.9 1.0
HD2 A:HIS527 3.2 24.7 1.0
CE1 A:HIS523 3.2 18.5 1.0
HE1 A:HIS527 3.3 19.8 1.0
HE1 A:HIS523 3.5 22.3 1.0
H19 A:IFW802 3.5 28.8 1.0
H10 A:IFW802 3.5 31.0 1.0
HH A:TYR607 3.5 23.5 1.0
HE2 A:TYR607 3.6 20.3 1.0
H26 A:IFW802 3.8 26.5 1.0
H8 A:IFW802 3.8 29.8 1.0
HA A:GLU555 4.0 19.8 1.0
ND1 A:HIS527 4.2 16.4 1.0
CG A:HIS527 4.2 17.1 1.0
OH A:TYR607 4.2 19.5 1.0
CG A:HIS523 4.2 16.8 1.0
C14 A:IFW802 4.3 22.3 1.0
CG A:GLU555 4.3 17.4 1.0
HB3 A:ALA558 4.3 17.8 1.0
CE2 A:TYR607 4.3 16.9 1.0
ND1 A:HIS523 4.3 18.3 1.0
O A:HOH920 4.3 23.6 1.0
C10 A:IFW802 4.4 25.8 1.0
OE1 A:GLU524 4.5 22.9 1.0
C16 A:IFW802 4.5 23.9 1.0
H7 A:IFW802 4.5 26.5 1.0
HB1 A:ALA558 4.5 17.8 1.0
HB3 A:GLU555 4.6 22.1 1.0
CZ A:TYR607 4.6 18.6 1.0
HG3 A:GLU555 4.7 21.0 1.0
H18 A:IFW802 4.7 26.3 1.0
C15 A:IFW802 4.7 21.9 1.0
CB A:ALA558 4.8 14.8 1.0
C8 A:IFW802 4.8 24.8 1.0
OE2 A:GLU524 4.8 29.2 1.0
HB2 A:ALA558 4.8 17.8 1.0
HG2 A:GLU555 4.8 21.0 1.0
CB A:GLU555 4.8 18.4 1.0
H16 A:IFW802 4.8 26.8 1.0
CA A:GLU555 4.8 16.5 1.0
HH A:TYR599 4.9 23.7 1.0
H24 A:IFW802 4.9 31.3 1.0
CD A:GLU524 4.9 23.1 1.0
C9 A:IFW802 4.9 29.3 1.0
HD1 A:HIS527 5.0 19.7 1.0

Reference:

A.Alhayek, A.S.Abdelsamie, E.Schonauer, V.Camberlein, E.Hutterer, G.Posselt, J.Serwanja, C.Blochl, C.G.Huber, J.Haupenthal, H.Brandstetter, S.Wessler, A.K.H.Hirsch. Discovery and Characterization of Synthesized and Fda-Approved Inhibitors of Clostridial and Bacillary Collagenases. J.Med.Chem. V. 65 12933 2022.
ISSN: ISSN 0022-2623
PubMed: 36154055
DOI: 10.1021/ACS.JMEDCHEM.2C00785
Page generated: Wed Oct 30 16:14:05 2024

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