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6TAK

Crystal structure of Escherichia coli Orotate Phosphoribosyltransferase in complex with Orotic acid and Sulfate at 1.25 Angstrom resolution

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000287molecular_functionmagnesium ion binding
AAA0004588molecular_functionorotate phosphoribosyltransferase activity
AAA0005737cellular_componentcytoplasm
AAA0005829cellular_componentcytosol
AAA0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
AAA0006221biological_processpyrimidine nucleotide biosynthetic process
AAA0016740molecular_functiontransferase activity
AAA0016757molecular_functionglycosyltransferase activity
AAA0042803molecular_functionprotein homodimerization activity
AAA0044205biological_process'de novo' UMP biosynthetic process
AAA0046132biological_processpyrimidine ribonucleoside biosynthetic process
BBB0000287molecular_functionmagnesium ion binding
BBB0004588molecular_functionorotate phosphoribosyltransferase activity
BBB0005737cellular_componentcytoplasm
BBB0005829cellular_componentcytosol
BBB0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
BBB0006221biological_processpyrimidine nucleotide biosynthetic process
BBB0016740molecular_functiontransferase activity
BBB0016757molecular_functionglycosyltransferase activity
BBB0042803molecular_functionprotein homodimerization activity
BBB0044205biological_process'de novo' UMP biosynthetic process
BBB0046132biological_processpyrimidine ribonucleoside biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VMLVDDVITAGtA
ChainResidueDetails
AAAVAL120-ALA132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01208","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01208","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01208","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8620002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01208","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8620002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 873
ChainResidueDetails

site_idMCSA2
Number of Residues2
DetailsM-CSA 873
ChainResidueDetails

243911

PDB entries from 2025-10-29

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