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4HMT

Crystal structure of PhzG from Pseudomonas fluorescens 2-79 in complex with hexahydrophenazine-1,6-dicarboxylic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0002047biological_processphenazine biosynthetic process
A0004733molecular_functionpyridoxamine phosphate oxidase activity
A0008615biological_processpyridoxine biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
A0017000biological_processantibiotic biosynthetic process
A0042816biological_processvitamin B6 metabolic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A1901615biological_processorganic hydroxy compound metabolic process
B0002047biological_processphenazine biosynthetic process
B0004733molecular_functionpyridoxamine phosphate oxidase activity
B0008615biological_processpyridoxine biosynthetic process
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
B0017000biological_processantibiotic biosynthetic process
B0042816biological_processvitamin B6 metabolic process
B0042823biological_processpyridoxal phosphate biosynthetic process
B1901615biological_processorganic hydroxy compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 301
ChainResidue
AARG73
AGLN152
ASER153
ANNV302
AHOH407
AHOH412
AHOH424
AHOH460
BLEU19
BTYR110
BGLN117
AILE74
BTRP195
BARG205
BHOH422
AVAL75
AVAL76
ASER88
ATHR89
ASER93
AGLN94
ALYS95

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NNV A 302
ChainResidue
ASER88
AHIS90
AARG139
ASER147
ATYR182
AFMN301
AHOH530
AHOH617
AHOH619
BSER18
BHIS203
BHOH485
BHOH585

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AGLN67
AARG69
AARG188

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AGLN31
AARG219

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AARG57
ASER78
AGLU79
AILE80
AHOH560

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 301
ChainResidue
ALEU19
ATYR110
AGLN117
ATRP195
AARG205
AHOH414
BARG73
BILE74
BVAL75
BVAL76
BSER88
BTHR89
BSER93
BGLN94
BLYS95
BGLN152
BSER153
BNNV302
BHOH416
BHOH432
BHOH434
BHOH453
BHOH488

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NNV B 302
ChainResidue
ASER18
ALEU19
AHIS203
AHOH607
AHOH635
BSER88
BHIS90
BARG139
BSER147
BFMN301

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BARG126
BASN129
BARG178
BGLU180
BGLY181
BHOH493

Functional Information from PROSITE/UniProt
site_idPS01064
Number of Residues14
DetailsPYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. LEFWGngqeRLHER
ChainResidueDetails
ALEU192-ARG205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23897464, ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV
ChainResidueDetails
ASER18
AARG139
BSER18
BARG139

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15502343, ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9, ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV
ChainResidueDetails
AARG73
BGLN117
BGLN152
BARG205
ASER88
AGLN94
AGLN117
AGLN152
AARG205
BARG73
BSER88
BGLN94

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23897464, ECO:0007744|PDB:4HMT
ChainResidueDetails
AHIS90
ASER147
BHIS90
BSER147

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PDB entries from 2024-07-24

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