Structure of PDB 3hyv Chain E

Receptor sequence
>3hyvE (length=429) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
AKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMG
WRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYL
VIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAI
PGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGA
SKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFM
PSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPI
EKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADF
GEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPS
FEEKVLEIFLKVHPIELCKDCEGAPGSRC
3D structure
PDB3hyv The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
ChainE
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E I8 G11 V12 S34 D35 R36 T42 P43 A78 T105 G106 P159 G293 V294 T313 G314 I317 I7 G10 V11 S33 D34 R35 T41 P42 A77 T104 G105 P158 G292 V293 T312 G313 I316
BS02 PS9 E C156 G158 P159 C155 G157 P158
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

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Cellular Component
External links
PDB RCSB:3hyv, PDBe:3hyv, PDBj:3hyv
PDBsum3hyv
PubMed19487671
UniProtO67931|SQRD_AQUAE Sulfide-quinone reductase (Gene Name=sqr)

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