Structure of PDB 6cin Chain E

Receptor sequence

>6cinE (length=1165) Species: 264732 (Moorella thermoacetica ATCC 39073)

PKQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFG
KTLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGE
LLPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLA
LVAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAF
RQRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGL
TGRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVR
LFRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGK
NILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSL
EIKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFV
YDSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGI
KPGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGL
GSRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTYGKKGDKILNMNFAA
VDRALEALEEIKYPASWADAVDEATEEPEFIQKVLRPINALKGDELPVST
FTPDGVFPVGTTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAIRPYL
AKPADLAGAPETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADVCPAK
VKALTMVPLEEVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQPLLEF
SGACAGCGETPYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYTVNRQ
GHGPAWASSLFEDNAEFGYGMALAVAKRQDELATAISKALEAPVSAAFKA
ACEGWLAGKDDADRSREYGDRIKALLPGEISQASGEVKDLLLDIDRQKDY
LTKKSIWIIGGDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNTGGQS
SKATQTGAVARFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHSQLMK
ALIEAEKYDGPSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLYRYNP
QLAQEGKNPFILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLFAKAE
ADAKARLEQYKKLAE

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): T29 E62 R112 N1000
• Catalytic site (residue number reindexed from 1): T28 E61 R111 N995
• 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	E	W681 C686 I687 C689 N690 C692 I735 C752 P753 A758 L759	W676 C681 I682 C684 N685 C687 I730 C747 P748 A753 L754
BS02	SF4	E	P679 C696 A700 I701 C742 T743 G744 C745 G746 C748	P674 C691 A695 I696 C737 T738 G739 C740 G741 C743
BS03	SF4	E	K456 A808 C809 C812 E814 C837 S999 C1075 I1076	K455 A803 C804 C807 E809 C832 S994 C1070 I1071
BS04	TPP	E	P27 I28 E62 E814 T835 G836 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P26 I27 E61 E809 T830 G831 C832 F861 G961 D962 G963 V992 Y993 S994 N995 T996
BS05	MG	E	D967 T995 V997	D962 T990 V992

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)