Structure of PDB 6cio Chain F

Receptor sequence

>6cioF (length=1155) Species: 264732 (Moorella thermoacetica ATCC 39073)

PKQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFG
KTLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGE
LLPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLA
LVAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAF
RQRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGL
TGRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVR
LFRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGK
NILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSL
EIKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFV
YDSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGI
KPGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGL
GSRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTYILNMNFAAVDRALE
ALEEIKYPASWADAVEEPEFIQKVLRPINALKGDELPVSTFTPDGVFPVG
TTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAIRPYLAKPADLAGAP
ETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADVCPAKVKALTMVPLE
EVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQPLLEFSGACAGCGET
PYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYTVNRQGHGPAWASSL
FEDNAEFGYGMALAVAKRQDELATAISKALEAPVSAAFKAACEGWLAGKD
DADRSREYGDRIKALLPGEISQASGEVKDLLLDIDRQKDYLTKKSIWIIG
GDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNTGGQSSKATQTGAVA
RFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHSQLMKALIEAEKYDG
PSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLYRYNPQLAQEGKNPF
ILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLFAKAEADAKARLEQY
KKLAE

3D structure

• PDB: 6cio Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromMoorella thermoacetica.
• Chain: F
• Resolution: 3.003 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T29 E62 R112 N1000
• Catalytic site (residue number reindexed from 1): T28 E61 R111 N985
• 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	W681 C686 I687 Q688 C689 N690 C692 C752 A758	W666 C671 I672 Q673 C674 N675 C677 C737 A743
BS02	SF4	F	P679 C696 A700 I701 C742 T743 G744 C745 G746 C748	P664 C681 A685 I686 C727 T728 G729 C730 G731 C733
BS03	SF4	F	K456 A808 C809 C812 E814 C837 S999 C1075 I1076	K455 A793 C794 C797 E799 C822 S984 C1060 I1061
BS04	TDL	F	P27 I28 T29 E62 Q86 R112 E814 T835 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P26 I27 T28 E61 Q85 R111 E799 T820 C822 F851 G951 D952 G953 V982 Y983 S984 N985 T986
BS05	MG	F	D967 T995 V997	D952 T980 V982

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