Structure of PDB 1mzy Chain A Binding Site BS03
Receptor Information
>1mzy Chain A (length=331) Species:
1063
(Cereibacter sphaeroides) [
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LSNLPRVKHTLVPPPFAHAHEQVAASGPVINEFEMRIIEKEVQLDEDAYL
QAMTFDGSIPGPLMIVHEGDYVELTLINPPENTMPHNIDFHAATGALGGG
GLTLINPGEKVVLRFKATRAGAFVYHCAPGGPMIPWHVVSGMAGCIMVLP
RDGLKDHEGKPVRYDTVYYIGESDHYIPKDEDGTYMRFSDPSEGYEDMVA
VMDTLIPSHIVFNGAVGALTGEGALKAKVGDNVLFVHSQPNRDSRPHLIG
GHGDLVWETGKFHNAPERDLETWFIRGGTAGAALYKFLQPGVYAYVNHNL
IEAVHKGATAHVLVEGEWDNDLMEQVVAPVG
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1mzy Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1mzy
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
Resolution
1.46 Å
Binding residue
(original residue number in PDB)
D220 T224
Binding residue
(residue number reindexed from 1)
D180 T184
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H126 D129 H131 H166 C167 H177 M182 H287 E311 T312 H338
Catalytic site (residue number reindexed from 1)
H86 D89 H91 H126 C127 H137 M142 H247 E271 T272 H298
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1mzy
,
PDBe:1mzy
,
PDBj:1mzy
PDBsum
1mzy
PubMed
UniProt
Q53239
|NIR_CERS5 Copper-containing nitrite reductase (Gene Name=nirK)
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