Structure of PDB 8rg9 Chain A

Receptor sequence
>8rg9A (length=338) Species: 566679 (Bradyrhizobium sp. ORS 375) [Search protein sequence]
DLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGTT
FQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALGG
GALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMVL
PRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDTE
EVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHLI
GGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHN
LIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGST
3D structure
PDB8rg9 Spectroscopically validated pH-dependent MSOX movies provide detailed mechanism of copper nitrite reductases.
ChainA
Resolution1.25 Å
3D
structure
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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 GLC A T52 F188 S190 T50 F186 S188
BS02 GLC A Y258 K289 Y256 K287
BS03 GLC A K49 R182 K47 R180
BS04 FRU A K185 G186 N187 K183 G184 N185
BS05 CU A H89 C130 H140 M145 H87 C128 H138 M143
BS06 CU A H94 H129 H92 H127
BS07 NO2 A D92 H94 H129 D90 H92 H127
BS08 NO2 A P88 M136 H140 P86 M134 H138
BS09 NO2 A K43 T52 S190 Y191 K41 T50 S188 Y189
BS10 NO A Q9 R10 Q7 R8
Gene Ontology
Molecular Function
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:8rg9, PDBe:8rg9, PDBj:8rg9
PDBsum8rg9
PubMed39002715
UniProtH0SLX7

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