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Calcium in PDB 1gm9: Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism

Enzymatic activity of Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism

All present enzymatic activity of Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism:
3.5.1.11;

Protein crystallography data

The structure of Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism, PDB code: 1gm9 was solved by C.E.Mcvey, M.A.Walsh, G.G.Dodson, K.S.Wilson, J.A.Brannigan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.200, 131.700, 64.000, 90.00, 105.90, 90.00
R / Rfree (%) 15.3 / 19

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism (pdb code 1gm9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism, PDB code: 1gm9:

Calcium binding site 1 out of 1 in 1gm9

Go back to Calcium Binding Sites List in 1gm9
Calcium binding site 1 out of 1 in the Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structures of Penicillin Acylase Enzyme-Substrate Complexes: Structural Insights Into the Catalytic Mechanism within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1568

b:10.9
occ:1.00
 OE2 A:GLU152 2.3 9.8 1.0
OD1 B:ASP76 2.3 8.6 1.0
O B:VAL75 2.4 8.6 1.0
OD2 B:ASP252 2.4 8.4 1.0
O B:PRO205 2.5 8.8 1.0
OD1 B:ASP73 2.6 8.3 1.0
OD2 B:ASP73 2.6 10.3 1.0
CG B:ASP73 2.9 11.5 1.0
CD A:GLU152 3.4 15.8 1.0
C B:VAL75 3.5 11.2 1.0
CG B:ASP252 3.5 10.2 1.0
CG B:ASP76 3.5 9.4 1.0
C B:PRO205 3.7 11.4 1.0
CA B:ASP76 3.8 11.5 1.0
CB B:ASP252 3.8 8.6 1.0
O B:HOH2194 4.0 9.8 1.0
CG A:GLU152 4.0 10.4 1.0
N B:ASP76 4.0 9.3 1.0
CB B:ASP76 4.1 7.5 1.0
NH2 B:ARG199 4.1 10.5 1.0
O A:HOH2135 4.2 9.8 1.0
CA B:PRO205 4.4 10.3 1.0
CB B:PRO205 4.4 10.2 1.0
OG1 A:THR150 4.4 8.1 1.0
OE1 A:GLU152 4.4 10.9 1.0
CB B:ASP73 4.5 9.3 1.0
OD2 B:ASP76 4.5 10.3 1.0
OD1 B:ASP252 4.6 10.7 1.0
CA B:VAL75 4.6 8.9 1.0
N B:VAL75 4.7 8.1 1.0
N B:ARG206 4.7 11.0 1.0
O2 B:EDO1564 4.7 15.2 1.0
CA B:ARG206 4.9 8.1 1.0

Reference:

C.E.Mcvey, M.A.Walsh, G.G.Dodson, K.S.Wilson, J.A.Brannigan. Crystal Structures of Penicillin Acylase Enzyme- Substrate Complexes: Structural Insights Into the Catalytic Mechanism J.Mol.Biol. V. 313 139 2001.
ISSN: ISSN 0022-2836
PubMed: 11601852
DOI: 10.1006/JMBI.2001.5043
Page generated: Thu Jul 11 08:44:22 2024

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