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Ligands
Code Name Style Show Link
JW5 6-(hydroxymethyl)uridine 5'-(dihydrogen phosphate)
Non-standard Residues
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CSS S-mercaptocysteine
Glycosylation
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Code : 2QCM   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Crystal structure of the orotidine-5'-monophosphate decarboxylase domain (Asp312Asn mutant) of human UMP synthase bound to 6-hydroxymethyl-UMP
Release Data : 2007-11-06
Compound :
mol_id molecule chains
1 Uridine 5'-monophosphate synthase (UMP synthase) A
ec: 4.1.1.23
fragment: C-terminal domain
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: UMPS
expression_system_strain: BL21 Rosetta 2(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pETM-30
Authors : Wittmann, J., Rudolph, M.
Keywords : UMP synthase, decarboxylase, catalytic proficiency, Lyase
Exp. method : X-RAY DIFFRACTION ( 1.67 Å )
Citation :

Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design.

Wittmann, J.G.,Heinrich, D.,Gasow, K.  et al.
(2008)  Structure  16 : 82 - 92

PubMed: 18184586
DOI: 10.1016/j.str.2007.10.020

Chain : A
UniProt : P11172 (UMPS_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D- ribose 1-diphosphate + orotate 2.4.2.10 PubMed:9042911
right-to-left
H(+) + orotidine 5'-phosphate = CO2 + UMP 4.1.1.23 PubMed:18184586, PubMed:9042911
left-to-right