Structure of PDB 7plm Chain A

Receptor sequence

>7plmA (length=1177) Species: 873 (Desulfocurvibacter africanus)

GKKMMTTDGNTATAHVAYAMSEVAAIYPITPSSTMGEEADDWAAQGRKNI
FGQTLTIREMQSEAGAAGAVHGALAAGALTTTFTASQGLLLMIPNMYKIS
GELLPGVFHVTARAIAAHALSIFGDHQDIYAARQTGFAMLASSSVQEAHD
MALVAHLAAIESNVPFMHFFDGFRTSHEIQKIEVLDYADMASLVNQKALA
EFRAKSMNPEHPHVRGTAQNPDIYFQGREAANPYYLKVPGIVAEYMQKVA
SLTGRSYKLFDYVGAPDAERVIVSMGSSCETIEEVINHLAAKGEKIGLIK
VRLYRPFVSEAFFAALPASAKVITVLDRTKEPGAPGDPLYLDVCSAFVER
GEAMPKILAGRYGLGSKEFSPAMVKSVYDNMSGAKKNHFTVGIEDDVTGT
SLPVDNAFADTTPKGTIQCQFWGLGADGTVGANKQAIKIIGDNTDLFAQG
YFSYDSKKSGGITISHLRFGEKPIQSTYLVNRADYVACHNPAYVGIYDIL
EGIKDGGTFVLNSPWSSLEDMDKHLPSGIKRTIANKKLKFYNIDAVKIAT
DVGRINMIMQTAFFKLAGVLAVDLLKKSIHKAIVKMNTDAVDQAVTSLQE
FKYPDSWKDANEFFKNVVKPILTQQGDKLPVSAFEADGRFPLGTSQFEKR
GVAINVPQWVPENCIQCNQCAFVCPHSAILPVLAKEEELNFTALEAKGKE
LKGYKFRIQINTLDCMGCGNCADICPPKEKALVMQPLDTQRDAQVPNLEY
AARIPVKSEVLPRDSLKGSQFQEPLMEFSGACSGCGETPYVRVITQLFGE
RMFIANATGCSSIWGASAPSMPYKTNRLGQGPAWGNSLFEDAAEYGFGMN
MSMFARRTHLADLAAKALESGDVKEALQGWLAGKNDPIKSKEYGDKLKKL
LAGQKDGLLGQIAAMSDLYTKKSVWIFGGDGWAYDIGYGGLDHVLASGED
VNVFVMDTEVYSNTGGQSSKATPTGAVAKFAAAGKRTGKKDLARMVMTYG
YVYVATVSMGYSKQQFLKVLKEAESFPGPSLVIAYATCINQGLRKGMGKS
QDVMNTAVKSGYWPLFRYDPRNPFQLDSKAPDGSVEEFLMAQNRFAVLDR
SFPEDAKRLRAQVAHELDVRFKELEHMAATGSVDFGEGAEFCTRDDTPMM
ARPDSGEACDQNRAGTSEQQGDLSKRT

3D structure

• PDB: 7plm Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy.
• Chain: A
• Resolution: 2.9 Å

Enzymatic activity

• 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	A	W684 C689 I690 Q691 C692 N693 C695 I738 C755 P756 A761 L762	W659 C664 I665 Q666 C667 N668 C670 I708 C725 P726 A731 L732
BS02	SF4	A	P682 C699 P700 I704 C745 M746 G747 C748 G749 C751	P657 C674 P675 I679 C715 M716 G717 C718 G719 C721
BS03	SF4	A	K459 A811 C812 C815 E817 C840 S995 C1071 I1072	K458 A781 C782 C785 E787 C810 S962 C1038 I1039
BS04	TPP	A	Y28 P29 I30 E64 E817 T838 G839 C840 F869 G962 D963 G964 V993 Y994 S995 N996 T997	Y27 P28 I29 E63 E787 T808 G809 C810 F839 G929 D930 G931 V960 Y961 S962 N963 T964
BS05	CA	A	D983 N985 F1059 G1061	D950 N952 F1026 G1028
BS06	MG	A	D963 T991 V993 S995	D930 T958 V960 S962

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

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:7plm, PDBe:7plm, PDBj:7plm
• PDBsum: 7plm
• PubMed: 35327633
• UniProt: P94692|PFOR_DESAF Pyruvate:ferredoxin oxidoreductase (Gene Name=por)