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2PRZ

S. cerevisiae orotate phosphoribosyltransferase complexed with OMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004588molecular_functionorotate phosphoribosyltransferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0044205biological_process'de novo' UMP biosynthetic process
A0046132biological_processpyrimidine ribonucleoside biosynthetic process
B0004588molecular_functionorotate phosphoribosyltransferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0044205biological_process'de novo' UMP biosynthetic process
B0046132biological_processpyrimidine ribonucleoside biosynthetic process
C0004588molecular_functionorotate phosphoribosyltransferase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0044205biological_process'de novo' UMP biosynthetic process
C0046132biological_processpyrimidine ribonucleoside biosynthetic process
D0004588molecular_functionorotate phosphoribosyltransferase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0044205biological_process'de novo' UMP biosynthetic process
D0046132biological_processpyrimidine ribonucleoside biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1
ChainResidue
ATYR75
ALYS76
BARG105

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 2
ChainResidue
CTYR75
CLYS76

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 225
ChainResidue
CARG105
DTYR75
DLYS76

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 225
ChainResidue
BTYR75
BLYS76
AARG105

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE OMP A 450
ChainResidue
ALEU28
ALYS29
APHE37
APHE38
AASP132
AVAL133
AMET134
ATHR135
AALA136
AGLY137
ATHR138
AALA139
AARG163
AHOH453
AHOH457
AHOH458
AHOH465
AHOH482
AHOH501

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE OMP B 550
ChainResidue
BLEU28
BLYS29
BPHE37
BPHE38
BASP132
BVAL133
BMET134
BTHR135
BALA136
BGLY137
BTHR138
BALA139
BARG163
BHOH554
BHOH559
BHOH560
BHOH577

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE OMP C 650
ChainResidue
CLEU28
CLYS29
CPHE37
CPHE38
CASP132
CVAL133
CMET134
CTHR135
CALA136
CGLY137
CTHR138
CALA139
CARG163
CHOH652
CHOH654
CHOH671
CHOH698
CHOH718
CHOH728

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE OMP D 750
ChainResidue
DLEU28
DLYS29
DPHE37
DPHE38
DASP132
DVAL133
DMET134
DTHR135
DALA136
DGLY137
DTHR138
DALA139
DARG163
DHOH753
DHOH754
DHOH756
DHOH787
DHOH815
DHOH835

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. ILIIDDVMTAGtA
ChainResidueDetails
AILE127-ALA139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsBinding site: {"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l1r
ChainResidueDetails
ALYS76

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l1r
ChainResidueDetails
BLYS76

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l1r
ChainResidueDetails
CLYS76

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l1r
ChainResidueDetails
DLYS76

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PDB entries from 2025-10-08

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