Structure of PDB 6x89 Chain S1 Binding Site BS04

Receptor Information
>6x89 Chain S1 (length=688) Species: 157791 (Vigna radiata) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PRSPLAGARVHFANPDDAIEVFVDGYPVKIPKGMTVLQACEVAGVDIPRF
CYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPVAKKAR
EGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEVKRSVVDK
NLGPLVKTVMTRCIQCTRCVRFATEVAGVQDLGMLGRGSGEEIGTYVEKL
LTSELSGNVIDICPVGALTSKPFAFKARNWELKGTETIDVTDAVGSNIRI
DSRGPEVMRIVPRLNEDINEEWISDKTRFCYDGLKRQRLNDPMIRGPDGR
FKAVNWRDALSVIADIAHQVKPEEIVGVAGKLSDAESMIALKDFLNRMGS
NDVWGEGIGVNTNADFRSGYIMNTSIAGLEKADVFLLVGTQPRVEAAMVN
ARIRKTVRSNQAKVGYIGPATDFNYDHKHLGTDPQTLVEIAEGRHPFFKT
LSDAKNPVIIVGAGVFERKDQDAIFAAVETIAQKANVVRPDWNGLNVLLL
HAAQAAALDLGLVPQSEKSLESAKFVYLMGADDVNLDKIPDDAFVVYQGH
HGDKSVYRANVILPTAAFSEKEGTYQNTEGCTQQTLPAVPTVGDSRDDWK
IIRALSEVAGVRLPYDTIGAVRARIRNVAPNLVNVDEREPATLPSSLRPS
FTQKVDTTPFGTVIENFYMTDAITRASKIMAQCSATLL
Ligand information
Ligand IDFES
InChIInChI=1S/2Fe.2S
InChIKeyNIXDOXVAJZFRNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04[Fe]1S[Fe]S1
CACTVS 3.341
OpenEye OEToolkits 1.5.0		S1[Fe]S[Fe]1
FormulaFe2 S2
NameFE2/S2 (INORGANIC) CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain6x89 Chain S1 Residue 803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6x89 Atomic structure of a mitochondrial complex I intermediate from vascular plants.
Resolution3.9 Å
Binding residue
(original residue number in PDB)		C107 G116 C118 R119 C121 C135
Binding residue
(residue number reindexed from 1)		C51 G60 C62 R63 C65 C79
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003954 NADH dehydrogenase activity
GO:0008137 NADH dehydrogenase (ubiquinone) activity
GO:0016491 oxidoreductase activity
GO:0016651 oxidoreductase activity, acting on NAD(P)H
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0042773 ATP synthesis coupled electron transport
GO:0045333 cellular respiration
GO:1902600 proton transmembrane transport
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6x89, PDBe:6x89, PDBj:6x89
PDBsum6x89
PubMed32840211
UniProtA0A1S3TQ85

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