Structure of PDB 1kqf Chain A

Receptor sequence

>1kqfA (length=982) Species: 562 (Escherichia coli)

QARNYKLLRAKEIRNTCTYCSVGCGLLMYSLGDGAKNAREAIYHIEGDPD
HPVSRGALCPKGAGLLDYVNSENRLRYPEYRAPGSDKWQRISWEEAFSRI
AKLMKADRDANFIEKNEQGVTVNRWLSTGMLCASGASNETGMLTQKFARS
LGMLAVDNQARVCHGPTVASLAPTFGRGAMTNHWVDIKNANVVMVMGGNA
AEAHPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITF
LSGVLRYLIENNKINAEYVKHYTNASLLVRDDFAFEDGLFSGYDAEKRQY
DKSSWNYQLDENGYAKRDETLTHPRCVWNLLKEHVSRYTPDVVENICGTP
KADFLKVCEVLASTSAPDRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLG
NMGMAGGGVNALRGHSNIQGLTDLGLLSTSLPGYLTLPSEKQVDLQSYLE
ANTPKATLADQVNYWSNYPKFFVSLMKSFYGDAAQKENNWGYDWLPKWDQ
TYDVIKYFNMMDEGKVTGYFCQGFNPVASFPDKNKVVSCLSKLKYMVVID
PLVTETSTFWQNHGESNDVDPASIQTEVFRLPSTCFAEEDGSIANSGRWL
QWHWKGQDAPGEARNDGEILAGIYHHLRELYQSEGGKGVEPLMKMSWNYK
QPHEPQSDEVAKENNGYALEDLYDANGVLIAKKGQLLSSFAHLRDDGTTA
SSCWIYTGSWTEQGNQMANRDNSDPSGLGNTLGWAWAWPLNRRVLYNRAS
ADINGKPWDPKRMLIQWNGSKWTGNDIPDFGNAAPGTPTGPFIMQPEGMG
RLFAINKMAEGPFPEHYEPIETPLGTNPLHPNVVSNPVVRLYEQDALRMG
KKEQFPYVGTTYRLTEHFHTWTKHALLNAIAQPEQFVEISETLAAAKGIN
NGDRVTVSSKRGFIRAVAVVTRRLKPLNVNGQQVETVGIPIHWGFEGVAR
KGYIANTLTPNVGDANSQTPEYKAFLVNIEKA

3D structure

• PDB: 1kqf Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K94 C196 H197 L410 R446 G447 H448
• Catalytic site (residue number reindexed from 1): K61 C163 H164 L377 R413 G414 H415
• Enzyme Commision number: 1.17.5.3: formate dehydrogenase-N.

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	A	C50 C53 V55 C57 L91 C92 G95 V239	C17 C20 V22 C24 L58 C59 G62 V206
BS02	MGD	A	Y101 Q192 U196 L410 Q414 H448 G556 F557 N558 S562 D583 P584 T617 D649 T894 R896 H902 W904 N989 Y1005	Y68 Q159 U163 L377 Q381 H415 G523 F524 N525 S529 D550 P551 T584 D616 T861 R863 H869 W871 N956 Y972
BS03	MGD	A	K94 G230 G231 N232 A236 D259 P260 R261 S277 D280 A409 L410 G411 H415 G447 T893 Y895 R896 L897 T898 H900 F901 H902 K1006	K61 G197 G198 N199 A203 D226 P227 R228 S244 D247 A376 L377 G378 H382 G414 T860 Y862 R863 L864 T865 H867 F868 H869 K973

Gene Ontology

Molecular Function

• GO:0008863 formate dehydrogenase (NAD+) activity
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0043546 molybdopterin cofactor binding
• GO:0047111 formate dehydrogenase (cytochrome-c-553) activity
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0045333 cellular respiration

External links

• PDB: RCSB:1kqf, PDBe:1kqf, PDBj:1kqf
• PDBsum: 1kqf
• PubMed: 11884747
• UniProt: P24183|FDNG_ECOLI Formate dehydrogenase, nitrate-inducible, major subunit (Gene Name=fdnG)