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1G77

X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004733molecular_functionpyridoxamine phosphate oxidase activity
A0005829cellular_componentcytosol
A0006725biological_processcellular aromatic compound metabolic process
A0008615biological_processpyridoxine biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
A0030170molecular_functionpyridoxal phosphate binding
A0032991cellular_componentprotein-containing complex
A0036001biological_process'de novo' pyridoxal 5'-phosphate biosynthetic process
A0042301molecular_functionphosphate ion binding
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A1901615biological_processorganic hydroxy compound metabolic process
A1902444molecular_functionriboflavin binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 280
ChainResidue
AARG23
AARG24
AARG120
AALA152
AARG153
AARG215
AHOH310
AHOH329
AHOH336

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 290
ChainResidue
ASER148
AARG149

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN A 250
ChainResidue
AARG67
AILE68
AVAL69
ALEU70
ATYR82
ATHR83
ASER87
AARG88
ALYS89
AGLN111
AGLN146
ASER147
ATRP191
AARG201
APLP260
AHOH308
AHOH312
AHOH322

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PLP A 260
ChainResidue
ALYS72
ATYR129
AARG133
AGLN146
AARG197
AHIS199
APRO218
AFMN250
AHOH338

Functional Information from PROSITE/UniProt
site_idPS01064
Number of Residues14
DetailsPYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. IEFWQggehRLHDR
ChainResidueDetails
AILE188-ARG201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11786019
ChainResidueDetails
AARG14
AARG197

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270
ChainResidueDetails
AARG67
ATYR82
AARG88
ALYS89
AGLN146

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11453690
ChainResidueDetails
ALYS72
ATYR129
AARG133
ASER137

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270
ChainResidueDetails
AGLN111
AARG201

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15858270
ChainResidueDetails
ATRP191

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 677
ChainResidueDetails
AARG197steric role

217705

PDB entries from 2024-03-27

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