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PDBsum entry 2v30
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* Residue conservation analysis
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PDB id:
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Lyase
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Title:
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Human orotidine 5'-phosphate decarboxylase domain of uridine monophospate synthetase (umps) in complex with its product ump.
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Structure:
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Orotidine 5'-phosphate decarboxylase. Chain: a, b. Fragment: orotidine 5'-phosphate decarboxylase domain, residues 224- 479. Synonym: ompdecase, uridine monophosphate synthetase-umps. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: mammalian gene collection (mgc)
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Resolution:
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2.00Å
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R-factor:
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0.155
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R-free:
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0.188
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Authors:
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M.Moche,D.Ogg,C.Arrowsmith,H.Berglund,R.Busam,R.Collins,L.G.Dahlgren, A.Edwards,S.Flodin,A.Flores,S.Graslund,M.Hammarstrom,B.M.Hallberg, L.Holmberg-Schiavone,I.Johansson,A.Kallas,T.Karlberg,T.Kotenyova, L.Lehtio,T.Nyman,C.Persson,J.Sagemark,P.Stenmark,M.Sundstrom, A.G.Thorsell,S.Van Den Berg,J.Weigelt,M.Welin,P.Nordlund,Structural Genomics Consortium (Sgc)
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Key ref:
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M.Moche
et al.
The crystal structure of human orotidine 5'- Decarboxylase domain of human uridine monophosphate synthetase (umps).
To be published,
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Date:
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10-Jun-07
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Release date:
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24-Jul-07
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PROCHECK
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Headers
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References
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P11172
(UMPS_HUMAN) -
Uridine 5'-monophosphate synthase from Homo sapiens
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Seq: Struc:
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480 a.a.
262 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 6 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.4.2.10
- orotate phosphoribosyltransferase.
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Pathway:
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Pyrimidine Biosynthesis
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Reaction:
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orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
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orotidine 5'-phosphate
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+
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diphosphate
Bound ligand (Het Group name = )
matches with 87.50% similarity
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=
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orotate
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+
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5-phospho-alpha-D-ribose 1-diphosphate
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Enzyme class 2:
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E.C.4.1.1.23
- orotidine-5'-phosphate decarboxylase.
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Pathway:
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Reaction:
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orotidine 5'-phosphate + H+ = UMP + CO2
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orotidine 5'-phosphate
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H(+)
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=
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UMP
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+
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CO2
Bound ligand (Het Group name = )
corresponds exactly
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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