Structure of PDB 2dv6 Chain F

Receptor sequence
>2dv6F (length=422) Species: 53399 (Hyphomicrobium denitrificans) [Search protein sequence]
HAPVVFTLRTGIAEGRMVYIGVGGDIDHKINPTLVVHEGETVQVNLVNGE
GAQHDVVVDQYAARSAIVNGKNASSTFSFVASKVGEFNYYCSIAGHRQAG
MEGNIQVLPGNRAEMKSSGADITRDPADLPGPIGPRQAKTVRIDLETVEV
KGQLDDNTTYTYWTFNGKVPGPFLRVRVGDTVELHLKNHKDSLMVHSVDF
HGATGPGGAAAFTQTDPGEETVVTFKALIPGIYVYHCATPSVPTHITNGM
YGLLLVEPEGGLPQVDREFYVMQGEIYTVKSFGTSGEQEMDYEKLINEKP
EYFLFNGSVGSLTRSHPLYASVGETVRIFFGVGGPNFTSSFHVIGEIFDH
VYSLGSVVSPPLIGVQTVSVPPGGATIVDFKIDRAGRYILVDHALSRLEH
GLVGFLNVDGPKNDSIMHEGPA
3D structure
PDB2dv6 Structure and function of a hexameric copper-containing nitrite reductase.
ChainF
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H219 D222 H224 H259 C260 H268 M273 H365 Q389 T390 H416
Catalytic site (residue number reindexed from 1) H196 D199 H201 H236 C237 H245 M250 H342 Q366 T367 H393
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
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 CU F H219 C260 H268 M273 H196 C237 H245 M250
BS02 CU F H224 H259 H201 H236
BS03 CU F H77 C114 H119 H54 C91 H96
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:2dv6, PDBe:2dv6, PDBj:2dv6
PDBsum2dv6
PubMed17360521
UniProtQ8KKH4

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