Structure of PDB 6cin Chain F

Receptor sequence

>6cinF (length=1158) Species: 264732 (Moorella thermoacetica ATCC 39073)

KQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFGK
TLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGEL
LPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLAL
VAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAFR
QRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGLT
GRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVRL
FRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGKN
ILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSLE
IKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFVY
DSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGIK
PGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGLG
SRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTMNFAAVDRALEALEEI
KYPASWADAVDEAAATVTEEPEFIQKVLRPINALKGDELPVSTFTPDGVF
PVGTTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAIRPYLAKPADLA
GAPETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADVCPAKVKALTMV
PLEEVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQPLLEFSGACAGC
GETPYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYTVNRQGHGPAWA
SSLFEDNAEFGYGMALAVAKRQDELATAISKALEAPVSAAFKAACEGWLA
GKDDADRSREYGDRIKALLPGEISQASGEVKDLLLDIDRQKDYLTKKSIW
IIGGDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNTGGQSSKATQTG
AVARFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHSQLMKALIEAEK
YDGPSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLYRYNPQLAQEGK
NPFILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLFAKAEADAKARL
EQYKKLAE

3D structure

• PDB: 6cin Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromMoorella thermoacetica.
• Chain: F
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T29 E62 R112 N1000
• Catalytic site (residue number reindexed from 1): T27 E60 R110 N988
• Enzyme Commision number: 1.2.7.1: pyruvate 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	SF4	F	C686 I687 Q688 C689 N690 C692 C752 P753 A758	C674 I675 Q676 C677 N678 C680 C740 P741 A746
BS02	SF4	F	P679 C696 A700 I701 C742 T743 C745 G746 N747 C748	P667 C684 A688 I689 C730 T731 C733 G734 N735 C736
BS03	SF4	F	K456 A808 C809 C812 E814 C837 S999 C1075 I1076	K454 A796 C797 C800 E802 C825 S987 C1063 I1064
BS04	TPP	F	P27 I28 E62 Q86 E814 T835 G836 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P25 I26 E60 Q84 E802 T823 G824 C825 F854 G954 D955 G956 V985 Y986 S987 N988 T989
BS05	MG	F	D967 T995 V997	D955 T983 V985

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005506 iron ion binding
• GO:0016491 oxidoreductase activity
• GO:0016903 oxidoreductase activity, acting on the aldehyde or oxo group of donors
• GO:0019164 pyruvate synthase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0046872 metal ion binding
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0006086 acetyl-CoA biosynthetic process from pyruvate
• GO:0006979 response to oxidative stress
• GO:0022900 electron transport chain

External links

• PDB: RCSB:6cin, PDBe:6cin, PDBj:6cin
• PDBsum: 6cin
• PubMed: 29581263
• UniProt: Q2RMD6|PFOR_MOOTA Pyruvate:ferredoxin oxidoreductase (Gene Name=Moth_0064)