Structure of PDB 6cin Chain D

Receptor sequence

>6cinD (length=1157) Species: 264732 (Moorella thermoacetica ATCC 39073)

KQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFGK
TLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGEL
LPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLAL
VAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAFR
QRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGLT
GRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVRL
FRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGKN
ILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSLE
IKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFVY
DSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGIK
PGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGLG
SRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTDKILNMNFAAVDRALE
ALEEIKYPASWADAVVTEEPEFIQKVLRPINALKGDELPVSTFTPDGVFP
VGTTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAIRPYLAKPADLAG
APETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADVCPAKVKALTMVP
LEEVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQPLLEFSGACAGCG
ETPYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYTVNRQGHGPAWAS
SLFEDNAEFGYGMALAVAKRQDELATAISKALEAPVSAAFKAACEGWLAG
KDDADRSREYGDRIKALLPGEISQASGEVKDLLLDIDRQKDYLTKKSIWI
IGGDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNTGGQSSKATQTGA
VARFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHSQLMKALIEAEKY
DGPSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLYRYNPQLAQEGKN
PFILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLFAKAEADAKARLE
QYKKLAE

3D structure

• PDB: 6cin Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromMoorella thermoacetica.
• Chain: D
• 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 N987
• 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	D	W681 C686 I687 Q688 C689 N690 C692 C752 P753 A758	W668 C673 I674 Q675 C676 N677 C679 C739 P740 A745
BS02	SF4	D	P679 C696 A700 I701 C742 T743 G744 C745 G746 C748	P666 C683 A687 I688 C729 T730 G731 C732 G733 C735
BS03	SF4	D	A808 C809 C812 E814 C837 S999 C1075 I1076	A795 C796 C799 E801 C824 S986 C1062 I1063
BS04	TPP	D	P27 I28 E62 Q86 E814 T835 G836 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P25 I26 E60 Q84 E801 T822 G823 C824 F853 G953 D954 G955 V984 Y985 S986 N987 T988
BS05	MG	D	D967 T995 V997	D954 T982 V984

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)