Structure of PDB 1kqg Chain B

Receptor sequence

>1kqgB (length=289) Species: 562 (Escherichia coli)

AMETQDIIKRSATNSITPPSQVRDYKAEVAKLIDVSTCIGCKACQVACSE
WNDIRDEVGHCVGVYDNPADLSAKSWTVMRFSETEQNGKLEWLIRKDGCM
HCEDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFNIPRLN
KEDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIHFGTKKEMLELAEQRVA
KLKARGYEHAGVYNPEGVGGTHVMYVLHHADQPELYHGLPKDPKIDTSVS
LWKGALKPLAAAGFIATFAGLIFHYIGIGPNKEVDDDEE

3D structure

• PDB: 1kqg Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
• Chain: B
• Resolution: 2.8 Å

Enzymatic activity

• Enzyme Commision number: 1.2.1.2: Transferred entry: 1.17.1.9.

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	SF4	B	C39 I40 G41 C42 K43 C45 M80 C179 P180 I184	C38 I39 G40 C41 K42 C44 M79 C178 P179 I183
BS02	SF4	B	K32 C49 N53 T78 C160 T161 L162 C163 P173 C175	K31 C48 N52 T77 C159 T160 L161 C162 P172 C174
BS03	SF4	B	C100 M101 H102 C103 P106 C108 V126 C143 F145 I147 P148 K159	C99 M100 H101 C102 P105 C107 V125 C142 F144 I146 P147 K158
BS04	SF4	B	C112 P113 I118 C133 I134 G135 C136 G137 Y138 C139 V157	C111 P112 I117 C132 I133 G134 C135 G136 Y137 C138 V156
BS05	HEM	B	Y138 W253	Y137 W252

Gene Ontology

Molecular Function

• GO:0009055 electron transfer activity
• GO:0036397 formate dehydrogenase (quinone) activity
• GO:0046872 metal ion binding
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0006788 heme oxidation
• GO:0009061 anaerobic respiration
• GO:0015944 formate oxidation
• GO:0019645 anaerobic electron transport chain
• GO:0045333 cellular respiration

Cellular Component

• GO:0005886 plasma membrane
• GO:0009326 formate dehydrogenase complex
• GO:0016020 membrane

External links

• PDB: RCSB:1kqg, PDBe:1kqg, PDBj:1kqg
• PDBsum: 1kqg
• PubMed: 11884747
• UniProt: P0AAJ3|FDNH_ECOLI Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit (Gene Name=fdnH)