Structure of PDB 2fug Chain C

Receptor sequence

>2fugC (length=737) Species: 300852 (Thermus thermophilus HB8)

MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLV
RIGLIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPLD
CPTCDKGGACELQDRTVEYGLYEKLPVYTRFEFTRRHVDKHHPLSPFVIL
DRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFSGNI
TDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGELLR
IRAREVPEVNEIWICDAGRFGHEWADQNRLKTPLVRKEGRLVEATWEEAF
LALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQGRTA
APASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPPHRY
NHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEEREI
LLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARLLAE
RAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPPEEALK
GKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLPLSPAP
IENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAMGRLSF
RLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAWAHPETARAEALPE
GAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAA

3D structure

• PDB: 2fug Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
• Chain: C
• Resolution: 3.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A293 A376 A377 A509 P537 A538
• Catalytic site (residue number reindexed from 1): A267 A350 A351 A483 P509 A510
• Enzyme Commision number: 7.1.1.-

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	C	H115 D118 C119 C122 K124 C128 Q131 V232 G233	H97 D100 C101 C104 K106 C110 Q113 V206 G207
BS02	SF4	C	C181 I182 C184 C187 C230 L235	C155 I156 C158 C161 C204 L209
BS03	SF4	C	C256 C259 V261 G262 C263 I290 C291	C230 C233 V235 G236 C237 I264 C265
BS04	FES	C	C34 S35 G43 A44 C45 C48 C83	C34 S35 G43 A44 C45 C48 C65

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

External links

• PDB: RCSB:2fug, PDBe:2fug, PDBj:2fug
• PDBsum: 2fug
• PubMed: 16469879
• UniProt: Q56223|NQO3_THET8 NADH-quinone oxidoreductase subunit 3 (Gene Name=nqo3)