Structure of PDB 1diq Chain A

Receptor sequence

>1diqA (length=515) Species: 303 (Pseudomonas putida) [Search protein sequence]

AVLPKGVTQGEFNKAVQKFRALLGDDNVLVESDQLVPYNKIMMPVENAAH
APSAAVTATTVEQVQGVVKICNEHKIPIWTISTGRNFGYGSAAPVQRGQV
ILDLKKMNKIIKIDPEMCYALVEPGVTFGQMYDYIQENNLPVMLSFSAPS
AIAGPVGNTMDRGVGYTPYGEHFMMQCGMEVVLANGDVYRTGMGGVPGSN
TWQIFKWGYGPTLDGMFTQANYGICTKMGFWLMPKPPVFKPFEVIFEDEA
DIVEIVDALRPLRMSNTIPNSVVIASTLWEAGSAHLTRAQYTTEPGHTPD
SVIKQMQKDTGMGAWNLYAALYGTQEQVDVNWKIVTDVFKKLGKGRIVTQ
EEAGDTQPFKYRAQLMSGVPNLQEFGLYNWRGGGGSMWFAPVSEARGSEC
KKQAAMAKRVLHKYGLDYVAEFIVAPRDMHHVIDVLYDRTNPEETKRADA
CFNELLDEFEKEGYAVYRVNTRFQDRVAQSYGPVKRKLEHAIKRAVDPNN
ILAPGRSGIDLNNDF

3D structure

PDB

1diq Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.

Chain

Resolution

2.75 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	Y95 S156 D167 E177 E286 Y367 E380 Y384 S392 H436 Y473 R474 R512
Catalytic site (residue number reindexed from 1)	Y89 S150 D161 E171 E280 Y361 E374 Y378 S386 H430 Y467 R468 R506
Enzyme Commision number	1.17.9.1: 4-methylphenol dehydrogenase (hydroxylating).

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	FAD	A	W85 T86 S88 T89 G90 R91 N92 S153 A154 P155 A159 G160 G163 N164 M166 G169 V170 Y172 I230 C231 E380 F381 Y384 W394 R474 R512	W79 T80 S82 T83 G84 R85 N86 S147 A148 P149 A153 G154 G157 N158 M160 G163 V164 Y166 I224 C225 E374 F375 Y378 W388 R468 R506
BS02	PCR	A	Y95 Y172 W285 W394 V438	Y89 Y166 W279 W388 V432

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004458	D-lactate dehydrogenase (cytochrome) activity
GO:0008720	D-lactate dehydrogenase activity
GO:0016491	oxidoreductase activity
GO:0018695	4-cresol dehydrogenase (hydroxylating) activity
GO:0050660	flavin adenine dinucleotide binding
GO:0071949	FAD binding

	Biological Process
GO:1903457	lactate catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1diq, PDBe:1diq, PDBj:1diq
PDBsum	1diq
PubMed	10623531
UniProt	P09788\|DH4C_PSEPU 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit (Gene Name=pchF)

[Back to BioLiP]