Structure of PDB 3hyw Chain C

Receptor sequence

>3hywC (length=429) Species: 63363 (Aquifex aeolicus)

AKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMG
WRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYL
VIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAI
PGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGA
SKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFM
PSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPI
EKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADF
GEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPS
FEEKVLEIFLKVHPIELCKDCEGAPGSRC

3D structure

• PDB: 3hyw The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C124 C156 H193 C347 D350 K382
• Catalytic site (residue number reindexed from 1): C123 C155 H192 C346 D349 K381
• Enzyme Commision number: 1.8.5.4: bacterial sulfide:quinone reductase.

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	FAD	C	G9 G10 G11 V12 G13 S34 D35 R36 T42 P43 K77 A78 T105 G106 P159 G293 V294 T313 G314 I317	G8 G9 G10 V11 G12 S33 D34 R35 T41 P42 K76 A77 T104 G105 P158 G292 V293 T312 G313 I316
BS02	DCQ	C	M315 E318 I346 F385 L407	M314 E317 I345 F384 L406
BS03	PS9	C	C156 G158 P159 I348	C155 G157 P158 I347

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003955 NAD(P)H dehydrogenase (quinone) activity
• GO:0016491 oxidoreductase activity
• GO:0042802 identical protein binding
• GO:0048038 quinone binding
• GO:0070224 sulfide:quinone oxidoreductase activity

Biological Process

• GO:0019646 aerobic electron transport chain

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:3hyw, PDBe:3hyw, PDBj:3hyw
• PDBsum: 3hyw
• PubMed: 19487671
• UniProt: O67931|SQRD_AQUAE Sulfide-quinone reductase (Gene Name=sqr)