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Chlorine in PDB 2qce: Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride

Enzymatic activity of Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride

All present enzymatic activity of Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride:
4.1.1.23;

Protein crystallography data

The structure of Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride, PDB code: 2qce was solved by J.Wittmann, M.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.79 / 1.43
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 77.224, 116.912, 61.965, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 16.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride (pdb code 2qce). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride, PDB code: 2qce:

Chlorine binding site 1 out of 1 in 2qce

Go back to Chlorine Binding Sites List in 2qce
Chlorine binding site 1 out of 1 in the Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Orotidine-5'-Monophosphate Decarboxylase Domain of Human Ump Synthase Bound to Sulfate, Glycerol, and Chloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl482

b:12.9
occ:1.00
O A:HOH516 3.1 14.1 1.0
O A:HOH512 3.2 13.8 1.0
O A:HOH504 3.2 12.8 1.0
NZ A:LYS314 3.2 9.1 1.0
O A:HOH529 3.3 15.4 1.0
CE A:LYS314 3.6 10.2 1.0
CG A:PRO417 3.8 9.8 1.0
C1 A:GOL484 3.8 10.7 1.0
CB A:PRO417 4.2 10.1 1.0
CE A:MET371 4.5 14.6 1.0
O1 A:GOL484 4.5 10.0 1.0
OD2 A:ASP312 4.6 9.4 1.0
CG2 A:ILE401 5.0 11.8 1.0
C3 A:GOL484 5.0 13.2 1.0

Reference:

J.G.Wittmann, D.Heinrich, K.Gasow, A.Frey, U.Diederichsen, M.G.Rudolph. Structures of the Human Orotidine-5'-Monophosphate Decarboxylase Support A Covalent Mechanism and Provide A Framework For Drug Design. Structure V. 16 82 2008.
ISSN: ISSN 0969-2126
PubMed: 18184586
DOI: 10.1016/J.STR.2007.10.020
Page generated: Sat Dec 12 09:16:47 2020

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