Structure of PDB 4kns Chain F Binding Site BS01

Receptor Information
>4kns Chain F (length=285) Species: 228410 (Nitrosomonas europaea ATCC 19718) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTVQVTLHAVETDVAYDNKGSTYRAWTFDGKVPGPVVRVTEGDTVEFTLI
NDKNSKNSHSMDFHAARLDVVEDFESIKPGETKKYTFTADNPGVFFYHCG
SDPMIQHIARGMYGVIIVDPKDANALPKADREYVLIQAEHYENPDDKTAM
MQNKWSNVVFNGGVFKYDPVHDSEATSWLQAKPGERVRIYFVNAGPNELS
SLHPIAGIWDRVYPSGNPKNVQYALQSYLIGAGDAATLDLISPVEGANAI
VDHSMRHAHSGAIAVIMFTNDADPEAGRGENILIR
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain4kns Chain F Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4kns Characterization of a nitrite reductase involved in nitrifier denitrification.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
H83 C123 H131 M136
Binding residue
(residue number reindexed from 1)
H59 C99 H107 M112
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H83 D86 H88 H122 C123 H131 M136 H227 Q250 S251 H277
Catalytic site (residue number reindexed from 1) H59 D62 H64 H98 C99 H107 M112 H203 Q226 S227 H253
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:4kns, PDBe:4kns, PDBj:4kns
PDBsum4kns
PubMed23857587
UniProtQ82VX5

[Back to BioLiP]