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4RV4

2.65 Angstrom Resolution Crystal Structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor' in complex with 5-phospho-alpha-D-ribosyl diphosphate (PRPP)

Replaces:  3OSC
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004588molecular_functionorotate phosphoribosyltransferase activity
A0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004588molecular_functionorotate phosphoribosyltransferase activity
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0019856biological_processpyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004588molecular_functionorotate phosphoribosyltransferase activity
C0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006222biological_processUMP biosynthetic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0019856biological_processpyrimidine nucleobase biosynthetic process
C0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVEDLISTGgS
ChainResidueDetails
AVAL116-SER128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AARG94
CLYS98
CHIS100
CSER124
ALYS98
AHIS100
ASER124
BARG94
BLYS98
BHIS100
BSER124
CARG94

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AGLU120
BGLU120
CGLU120

218853

PDB entries from 2024-04-24

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