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1ORO

A FLEXIBLE LOOP AT THE DIMER INTERFACE IS A PART OF THE ACTIVE SITE OF THE ADJACENT MONOMER OF ESCHERICHIA COLI OROTATE PHOSPHORIBOSYLTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004588molecular_functionorotate phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0042803molecular_functionprotein homodimerization activity
A0044205biological_process'de novo' UMP biosynthetic process
A0046132biological_processpyrimidine ribonucleoside biosynthetic process
A0055086biological_processnucleobase-containing small molecule metabolic process
A0072528biological_processpyrimidine-containing compound biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004588molecular_functionorotate phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0042803molecular_functionprotein homodimerization activity
B0044205biological_process'de novo' UMP biosynthetic process
B0046132biological_processpyrimidine ribonucleoside biosynthetic process
B0055086biological_processnucleobase-containing small molecule metabolic process
B0072528biological_processpyrimidine-containing compound biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
AARG99
ALYS103
BALA71
BTYR72
BLYS73
BLYS100
BHOH516

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ALYS73
ALYS100
AHOH502
AHOH503
AHOH514
BARG99
AALA71
ATYR72

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VMLVDDVITAGtA
ChainResidueDetails
AVAL120-ALA132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
ASER27
AASP125
BSER27
BASP125

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
APHE35
AGLY106
AALA129
AGLN157
BPHE35
BGLY106
BALA129
BGLN157

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
ChainResidueDetails
ALYS73
AGLU101
BLYS73
BGLU101

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
ChainResidueDetails
ALYS100
AASP104
BLYS100
BASP104

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 873
ChainResidueDetails
AASP104electrostatic stabiliser, proton acceptor, proton donor
AGLY106electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 873
ChainResidueDetails
BASP104electrostatic stabiliser, proton acceptor, proton donor
BGLY106electrostatic stabiliser

220113

PDB entries from 2024-05-22

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