Structure of PDB 7zco Chain A

Receptor sequence
>7zcoA (length=341) Species: 566679 (Bradyrhizobium sp. ORS 375) [Search protein sequence]
DDLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGT
TFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALG
GGALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMV
LPRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDT
EEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHL
IGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTH
NLIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNE
3D structure
PDB7zco Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
ChainA
Resolution1.22 Å
3D
structure
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Enzymatic activity
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 FRU A K185 G186 N187 K184 G185 N186
BS02 CU A H89 C130 H140 M145 H88 C129 H139 M144
BS03 CU A H94 H129 H93 H128
BS04 NO A D92 H94 H129 D91 H93 H128
BS05 NO2 A P88 P132 M136 H140 P87 P131 M135 H139
BS06 NO2 A S61 M62 N216 S60 M61 N215
BS07 NO2 A D92 H94 H129 D91 H93 H128
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:7zco, PDBe:7zco, PDBj:7zco
PDBsum7zco
PubMed35862453
UniProtH0SLX7

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