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3M3H

1.75 Angstrom resolution crystal structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor'

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004588molecular_functionorotate phosphoribosyltransferase activity
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 211
ChainResidue
ATYR43
APRO44
ALYS45
AVAL46
AGLY188
AGLN189
AALA190
AHOH218

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 212
ChainResidue
AGLY126
ASER128
AALA129
ASER124

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 213
ChainResidue
AARG137
AVAL143
AHOH306

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 214
ChainResidue
APHE62
APRO63
ATHR64
AHOH327

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 215
ChainResidue
ACYS35
AASN37
AASP121

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 216
ChainResidue
AARG38
ATYR92
AARG94

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 217
ChainResidue
APRO44
AGLN189

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 Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AARG94
ALYS98
AHIS100
ASER124

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01208
ChainResidueDetails
AGLU120

225158

PDB entries from 2024-09-18

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