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6TAJ

Crystal structure of Escherichia coli Orotate Phosphoribosyltransferase in complex with Orotic acid 1.60 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
AAA0055086biological_processnucleobase-containing small molecule metabolic process
AAA0072528biological_processpyrimidine-containing compound 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
BBB0055086biological_processnucleobase-containing small molecule metabolic process
BBB0072528biological_processpyrimidine-containing compound 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 Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AAALYS26
AAAASP124
BBBLYS26
BBBASP124

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AAAPHE34
AAAHIS105
AAATHR128
AAAARG156
BBBPHE34
BBBHIS105
BBBTHR128
BBBARG156

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
ChainResidueDetails
AAATYR72
AAALYS100
BBBTYR72
BBBLYS100

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
ChainResidueDetails
AAAARG99
AAALYS103
BBBARG99
BBBLYS103

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 873
ChainResidueDetails
AAALYS103electrostatic stabiliser, proton acceptor, proton donor
AAAHIS105electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 873
ChainResidueDetails
BBBLYS103electrostatic stabiliser, proton acceptor, proton donor
BBBHIS105electrostatic stabiliser

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PDB entries from 2024-04-24

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