Structure of PDB 1krh Chain B

Receptor sequence

>1krhB (length=337) Species: 472 (Acinetobacter sp.)

SNHQVALQFEDGVTRFICIAQGETLSDAAYRQQINIPMDCREGECGTCRA
FCESGNYDMPEDNYIEDALTPEEAQQGYVLACQCRPTSDAVFQIQASSEV
CKTKIHHFEGTLARVENLSDSTITFDIQLDDGQPDIHFLAGQYVNVTLPG
TTETRSYSFSSQPGNRLTGFVVRNVPQGKMSEYLSVQAKAGDKMSFTGPF
GSFYLRDVKRPVLMLAGGTGIAPFLSMLQVLEQKGSEHPVRLVFGVTQDC
DLVALEQLDALQQKLPWFEYRTVVAHAESQHERKGYVTGHIEYDWLNGGE
VDVYLCGPVPMVEAVRSWLDTQGIQPANFLFEKFSAN

3D structure

• PDB: 1krh X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1.
• Chain: B
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C307
• Catalytic site (residue number reindexed from 1): C306
• Enzyme Commision number: 1.18.1.3: ferredoxin--NAD(+) reductase.

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	FES	B	M39 D40 C41 R42 G44 C46 G47 C49 C83	M38 D39 C40 R41 G43 C45 G46 C48 C82
BS02	FAD	B	Y144 R156 S157 Y158 S159 V173 G179 K180 M181 S182 T220 E333 K334 F335 S336 A337 N338	Y143 R155 S156 Y157 S158 V172 G178 K179 M180 S181 T219 E332 K333 F334 S335 A336 N337

Gene Ontology

Molecular Function

• GO:0008860 ferredoxin-NAD+ reductase activity
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0051536 iron-sulfur cluster binding
• GO:0051537 2 iron, 2 sulfur cluster binding

Biological Process

• GO:0009056 catabolic process
• GO:0042203 toluene catabolic process

External links

• PDB: RCSB:1krh, PDBe:1krh, PDBj:1krh
• PDBsum: 1krh
• PubMed: 12051836
• UniProt: P07771|BENC_ACIAD Benzoate 1,2-dioxygenase electron transfer component (Gene Name=benC)