Structure of PDB 6hl2 Chain D

Receptor sequence
>6hl2D (length=417) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
RSYPAIPRIYAETTLNMLLKRAKKPRVHSIDEYLKDGGYQALEKALNMSP
EEIIDWVDKSTLRGRGGAGFPTGKKWKFAVQNPGPRYFICNADESEPGTF
KDRIIIERDPHLLIEGIIISSYAIGANEAYIYIRGEYPAGYYILRDAIEE
AKKKGFLGKNILGSGFDLEIYVARGAGAYICGEETALIESLEGKRGHPRL
KPPYPVQKGLWGKPTVVNNVETIANVPFIISMGWEEYRYIGPSDYAGPKL
FPVSGKVKKPGVYELPMNTTLREVIFKYAGGTLGNKKVKAVFSGALDCFS
SEELDIPMDYSPLGFGGTGTVIVLTEEDDIVEAALKIAEFYEHETCGQCT
PCRVGCYEQANLLEKIYKGEATEQDWEGFDFVNRNIQPTSICGLGAVAGR
LIRQTLEKFPEEWEKYR
3D structure
PDB6hl2 A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.
ChainD
Resolution1.95 Å
3D
structure
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Enzymatic activity
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 D P199 T346 C347 G348 Q349 C350 C353 S391 I392 C393 G396 P198 T345 C346 G347 Q348 C349 C352 S390 I391 C392 G395
BS02 FMN D G65 G67 K76 N92 E95 G183 E184 E185 V218 N219 N220 T223 G394 G64 G66 K75 N91 E94 G182 E183 E184 V217 N218 N219 T222 G393
Gene Ontology
Molecular Function
GO:0008137 NADH dehydrogenase (ubiquinone) activity
GO:0010181 FMN binding
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:1902600 proton transmembrane transport

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Molecular Function
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Biological Process
External links
PDB RCSB:6hl2, PDBe:6hl2, PDBj:6hl2
PDBsum6hl2
PubMed31186428
UniProtO66841|NUOF_AQUAE NADH-quinone oxidoreductase subunit F (Gene Name=nuoF)

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