Structure of PDB 1mzz Chain A Binding Site BS02

Receptor Information
>1mzz Chain A (length=334) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDLSNLPRVKHTLVPPPFAHAHEQVAASGPVINEFEMRIIEKEVQLDEDA
YLQAMTFDGSIPGPLMIVHEGDYVELTLINPPENTMPHNIDFHAATGALG
GGGLTLINPGEKVVLRFKATRAGAFVYHCAPGGPMIPWHVVSGTAGCIMV
LPRDGLKDHEGKPVRYDTVYYIGESDHYIPKDEDGTYMRFSDPSEGYEDM
VAVMDTLIPSHIVFNGAVGALTGEGALKAKVGDNVLFVHSQPNRDSRPHL
IGGHGDLVWETGKFHNAPERDLETWFIRGGTAGAALYKFLQPGVYAYVNH
NLIEAVHKGATAHVLVEGEWDNDLMEQVVAPVGL
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 chain1mzz Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mzz The High resolution Crystal Structures of Nitrite Reductase and its mutant Met182Thr from Rhodobacter Sphaeroides Reveal a Gating Mechanism for the Electron Transfer to the Type 1 Copper Center
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H131 H166
Binding residue
(residue number reindexed from 1)		H93 H128
Annotation score1
Enzymatic activity
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
Biological Process
GO:0019333 denitrification pathway
GO:0042128 nitrate assimilation
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1mzz, PDBe:1mzz, PDBj:1mzz
PDBsum1mzz
PubMed
UniProtQ53239|NIR_CERS5 Copper-containing nitrite reductase (Gene Name=nirK)

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