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1NRG

Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004733molecular_functionpyridoxamine phosphate oxidase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
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
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0042818biological_processpyridoxamine metabolic process
A0042822biological_processpyridoxal phosphate metabolic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A1901615biological_processorganic hydroxy compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 340
ChainResidue
AGLU114
ALYS119
AGLN174
ASER175
AHOH495
AHOH579

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 300
ChainResidue
ALEU97
ALEU98
APHE110
ATHR111
ASER115
AARG116
ALYS117
ATYR132
AGLN139
AARG141
AGLN174
ASER175
ATRP219
AARG229
APLP320
AHOH428
AHOH429
AHOH436
AHOH465
AGLU77
AARG95
AMET96

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP A 320
ChainResidue
ALEU98
ALYS100
ATYR157
AARG161
ASER165
AGLN174
AARG225
AHIS227
APRO261
AFMN300

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 360
ChainResidue
ACYS72
APRO135

Functional Information from PROSITE/UniProt
site_idPS01064
Number of Residues14
DetailsPYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. MEFWQgqtnRLHDR
ChainResidueDetails
AMET216-ARG229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0AFI7
ChainResidueDetails
AARG42
AGLN139
ATRP219
AARG225
AARG229

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12824491
ChainResidueDetails
AARG95
ALYS100
APHE110
AARG116
ATYR157
AARG161
ASER165
AGLN174

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR238

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER241

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g79
ChainResidueDetails
AARG225

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PDB entries from 2024-11-13

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