Structure of PDB 4hmt Chain A

Receptor sequence

>4hmtA (length=205) Species: 294 (Pseudomonas fluorescens)

SLTGTLDAPFPEYQTLPADPMSVLHNWLERARRVGIREPRALALATADSQ
GRPSTRIVVISEISDAGVVFSTHAGSQKGRELLHNPWASGVLYWRETSQQ
IILNGQAVRLPNAKADDAWLKRPYATHPMSSVSRQSEELQDVQAMRNAAR
QLAELQGPLPRPEGYCVFELRLESLEFWGNGQERLHERLRYDRSDTGWNV
RRLQP

3D structure

• PDB: 4hmt Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis
• Chain: A
• Resolution: 1.42 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R201
• Catalytic site (residue number reindexed from 1): R184
• 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	A	R73 I74 V75 V76 S88 T89 S93 Q94 K95 Q152 S153	R56 I57 V58 V59 S71 T72 S76 Q77 K78 Q135 S136
BS02	NNV	A	S88 H90 R139 S147 Y182	S71 H73 R122 S130 Y165
BS03	FMN	A	Y110 Q117 W195 R205	Y93 Q100 W178 R188
BS04	NNV	A	S18 L19 H203	S1 L2 H186

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

External links

• PDB: RCSB:4hmt, PDBe:4hmt, PDBj:4hmt
• PDBsum: 4hmt
• PubMed: 23897464
• UniProt: Q51793|PHZG_PSEFL Dihydrophenazinedicarboxylate synthase (Gene Name=phzG)