Structure of PDB 4hmt Chain B

Receptor sequence
>4hmtB (length=207) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
SESLTGTLDAPFPEYQTLPADPMSVLHNWLERARRVGIREPRALALATAD
SQGRPSTRIVVISEISDAGVVFSTHAGSQKGRELLHNPWASGVLYWRETS
QQIILNGQAVRLPNAKADDAWLKRPYATHPMSSVSRQSEELQDVQAMRNA
ARQLAELQGPLPRPEGYCVFELRLESLEFWGNGQERLHERLRYDRSDTGW
NVRRLQP
3D structure
PDB4hmt Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis
ChainB
Resolution1.42 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R201
Catalytic site (residue number reindexed from 1) R186
Enzyme Commision number 1.10.3.16: dihydrophenazinedicarboxylate synthase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FMN B Y110 Q117 W195 R205 Y95 Q102 W180 R190
BS02 FMN B R73 I74 V75 V76 S88 T89 S93 Q94 K95 Q152 S153 R58 I59 V60 V61 S73 T74 S78 Q79 K80 Q137 S138
BS03 NNV B S88 H90 R139 S147 S73 H75 R124 S132
Gene Ontology
Molecular Function
GO:0004733 pyridoxamine phosphate oxidase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors
Biological Process
GO:0002047 phenazine biosynthetic process
GO:0008615 pyridoxine biosynthetic process
GO:0017000 antibiotic biosynthetic process
GO:0042816 vitamin B6 metabolic process
GO:0042823 pyridoxal phosphate biosynthetic process
GO:1901615 organic hydroxy compound metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4hmt, PDBe:4hmt, PDBj:4hmt
PDBsum4hmt
PubMed23897464
UniProtQ51793|PHZG_PSEFL Dihydrophenazinedicarboxylate synthase (Gene Name=phzG)

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