Structure of PDB 2fug Chain 3 Binding Site BS03

Receptor Information
>2fug Chain 3 (length=737) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLV
RIGLIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLD
CPTCDKGGACELQDRTVEYGLYEKLPVYTRFEFTRRHVDKHHPLSPFVIL
DRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNI
TDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLR
IRAREVPEVNEIWICDAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAF
LALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTA
APASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRY
NHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREI
LLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAE
RAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALK
GKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAP
IENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSF
RLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAWAHPETARAEALPE
GAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAA
Ligand information
Ligand IDSF4
InChIInChI=1S/4Fe.4S
InChIKeyLJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
FormulaFe4 S4
NameIRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain2fug Chain 3 Residue 786 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fug Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
Resolution3.3 Å
Binding residue
(original residue number in PDB)		C256 C259 V261 G262 C263 I290 C291
Binding residue
(residue number reindexed from 1)		C230 C233 V235 G236 C237 I264 C265
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A376 A377 A509 P537 A538
Catalytic site (residue number reindexed from 1) A350 A351 A483 P509 A510
Enzyme Commision number 7.1.1.-
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:0043546 molybdopterin cofactor binding
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0051536 iron-sulfur cluster binding
GO:0051537 2 iron, 2 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:0005886 plasma membrane
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:2fug, PDBe:2fug, PDBj:2fug
PDBsum2fug
PubMed16469879
UniProtQ56223|NQO3_THET8 NADH-quinone oxidoreductase subunit 3 (Gene Name=nqo3)

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