Structure of PDB 3ias Chain U

Receptor sequence

>3iasU (length=754) Species: 300852 (Thermus thermophilus HB8)

MVRVKVNDRIVEVPPGTSVMDAVFHAGYDVPLFCSEKHLSPIGACRMCLV
RIGLPIQWQPKLAASCVTAVADGMVVDTLSDVVREAQAGMVEFTLLNHPL
DCPTCDKGGACELQDRTVEYGLYEKYELPVYTRFEFTRRHVDKHHPLSPF
VILDRERCIHCKRCVRYFEEVPGDEVLDFIERGVHTFIGTMDFGLPSGFS
GNITDICPVGALLDLTARFRARNWEMEETPTTCALCPVGCGITADTRSGE
LLRIRAREVPEVNEIWICDAGRFGHEWADQNRLKTPLVRKEGRLVEATWE
EAFLALKEGLKEARGEEVGLYLAHDATLEEGLLASELAKALKTPHLDFQG
RTAAPASLFPPASLEDLLQADFALVLGDPTEEAPILHLRLSEFVRDLKPP
HRYNHGTPFADLQIKERMPRRTDKMALFAPYRAPLMKWAAIHEVHRPGEE
REILLALLGDKEGSEMVAKAKEAWEKAKNPVLILGAGVLQDTVAAERARL
LAERKGAKVLAMTPAANARGLEAMGVLPGAKGASWDEPGALYAYYGFVPP
EEALKGKRFVVMHLSHLHPLAERYAHVVLPAPTFYEKRGHLVNLEGRVLP
LSPAPIENGEAEGALQVLALLAEALGVRPPFRLHLEAQKALKARKVPEAM
GRLSFRLKELRPKERKGAFYLRPTMWKAHQAVGKAQEAARAELWAHPETA
RAEALPEGAQVAVETPFGRVEARVVHREDVPKGHLYLSALGPAAGLRVEG
RVLV

3D structure

• PDB: 3ias Structural basis for the mechanism of respiratory complex I
• Chain: U
• Resolution: 3.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A376 A377 A509 P537 A538
• Catalytic site (residue number reindexed from 1): A353 A354 A486 P514 A515
• 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	U	H115 D118 C119 C122 K124 C128 L130 Q131 V232	H98 D101 C102 C105 K107 C111 L113 Q114 V209
BS02	SF4	U	C181 I182 C184 C187 F202 I211 C230 P231 L235	C158 I159 C161 C164 F179 I188 C207 P208 L212
BS03	SF4	U	C256 C259 V261 G262 C263 I290 C291 G294 P407	C233 C236 V238 G239 C240 I267 C268 G271 P384
BS04	FES	U	C34 S35 G43 C45 R46 C48 C83	C34 S35 G43 C45 R46 C48 C66
BS05	CA	U	L274 D302	L251 D279

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:3ias, PDBe:3ias, PDBj:3ias
• PDBsum: 3ias
• PubMed: 19635800
• UniProt: Q56223|NQO3_THET8 NADH-quinone oxidoreductase subunit 3 (Gene Name=nqo3)