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Calcium in PDB 1t5h: 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine

Enzymatic activity of 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine

All present enzymatic activity of 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine:
6.2.1.33;

Protein crystallography data

The structure of 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine, PDB code: 1t5h was solved by A.M.Gulick, X.Lu, D.Dunaway-Mariano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 124.979, 124.979, 69.001, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 20.6

Calcium Binding Sites:

The binding sites of Calcium atom in the 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine (pdb code 1t5h). 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 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine, PDB code: 1t5h:

Calcium binding site 1 out of 1 in 1t5h

Go back to Calcium Binding Sites List in 1t5h
Calcium binding site 1 out of 1 in the 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 4-Chlorobenzoyl-Coa Ligase/Synthetase Unliganded, Selenomethionine within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca999

b:31.9
occ:1.00
OE1 X:GLN484 2.3 14.5 1.0
O X:HOH1184 2.4 30.2 1.0
O X:HOH1067 2.5 33.0 1.0
O X:HOH1183 2.5 32.2 1.0
OD2 X:ASP483 2.5 12.2 1.0
OD1 X:ASP483 2.6 12.0 1.0
CG X:ASP483 3.0 12.2 1.0
CD X:GLN484 3.4 15.5 1.0
CG X:GLN484 4.0 14.7 1.0
NE2 X:GLN484 4.5 16.0 1.0
CB X:ASP483 4.5 12.3 1.0
O X:HOH1330 4.6 37.9 1.0
O X:HOH1240 4.9 35.6 1.0

Reference:

A.M.Gulick, X.Lu, D.Dunaway-Mariano. Crystal Structure of 4-Chlorobenzoate:Coa Ligase/Synthetase in the Unliganded and Aryl Substrate-Bound States Biochemistry V. 43 8670 2004.
ISSN: ISSN 0006-2960
PubMed: 15236575
DOI: 10.1021/BI049384M
Page generated: Thu Jul 11 22:56:37 2024

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