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Zinc in PDB 1smp: Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi

Enzymatic activity of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi

All present enzymatic activity of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi:
3.4.24.40;

Protein crystallography data

The structure of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi, PDB code: 1smp was solved by U.Baumann, M.Bauer, S.Letoffe, P.Delepelaire, C.Wandersman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 108.830, 108.830, 87.950, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 24.7

Other elements in 1smp:

The structure of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi also contains other interesting chemical elements:

Calcium (Ca) 7 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi (pdb code 1smp). 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 A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi, PDB code: 1smp:

Zinc binding site 1 out of 1 in 1smp

Go back to Zinc Binding Sites List in 1smp
Zinc binding site 1 out of 1 in the Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi


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 A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn472

b:23.5
occ:1.00
 O I:SER1 1.9 6.1 0.5
NE2 A:HIS180 2.1 9.8 1.0
NE2 A:HIS186 2.2 23.4 1.0
NE2 A:HIS176 2.3 21.3 1.0
N I:SER1 2.8 13.1 0.5
C I:SER1 2.9 11.5 0.5
CD2 A:HIS180 2.9 12.8 1.0
CD2 A:HIS186 3.0 22.7 1.0
CD2 A:HIS176 3.1 23.6 1.0
CA I:SER1 3.3 12.0 0.5
CE1 A:HIS180 3.3 13.9 1.0
CE1 A:HIS186 3.4 22.9 1.0
CE1 A:HIS176 3.4 22.4 1.0
CB I:SER1 3.7 12.5 0.5
OE2 A:GLU177 4.0 15.9 1.0
N I:SER2 4.1 14.3 1.0
CG A:HIS180 4.1 12.3 1.0
O A:HOH647 4.1 62.5 1.0
O I:HOH305 4.2 42.0 1.0
CG A:HIS186 4.2 22.7 1.0
ND1 A:HIS180 4.3 12.6 1.0
OE1 A:GLU177 4.3 15.7 1.0
CG A:HIS176 4.3 24.2 1.0
CE1 A:TYR216 4.4 16.6 1.0
ND1 A:HIS186 4.4 24.2 1.0
OH A:TYR216 4.4 19.3 1.0
ND1 A:HIS176 4.4 23.4 1.0
CD A:GLU177 4.5 15.0 1.0
OG I:SER2 4.6 12.5 1.0
OG I:SER1 4.6 18.1 0.5
CA I:SER2 4.8 15.1 1.0
CE A:MET214 4.8 13.0 1.0
CZ A:TYR216 4.9 16.9 1.0

Reference:

U.Baumann, M.Bauer, S.Letoffe, P.Delepelaire, C.Wandersman. Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi. J.Mol.Biol. V. 248 653 1995.
ISSN: ISSN 0022-2836
PubMed: 7752231
DOI: 10.1006/JMBI.1995.0249
Page generated: Wed Oct 16 18:52:48 2024

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