Structure of PDB 3wi9 Chain A

Receptor sequence
>3wi9A (length=303) Species: 235909 (Geobacillus kaustophilus HTA426) [Search protein sequence]
TQQSAANMLAAHKGVNQAPVPLKMERVGPHDVHIEMTAQITDIEIDKGKI
YKAWTFNGQAPGPLVVVNEGDTIHFTLKNMDPVVPHSMDFHAVHASPSKD
FIDVMPNKSGTFTYPANKPGVFMYHCGTKPVLQHIANGMHGVIIVKPKNG
YPTDKEVDREYVLIQNEWYKYNDMNDFQNGVPSYVVFSSKALKPGDPNTN
GDTFTLKEKPLLAKVGEKIRLYINNVGPNEVSSFHVVGTVFDDVYLDGNP
NNHLQGMQTVMLPASGGAVVEFTVTRPGTYPIVTHQFNHAQKGAVAMLKV
TET
3D structure
PDB3wi9 Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H95 D98 H100 H134 C135 H143 M148 H244 Q267 T268 H294
Catalytic site (residue number reindexed from 1) H86 D89 H91 H125 C126 H134 M139 H235 Q258 T259 H285
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 CU A H95 C135 H143 M148 H86 C126 H134 M139
BS02 CU A H100 H134 H91 H125
BS03 ZN A H42 H83 H33 H74
BS04 ZN A H42 H83 H33 H74
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:3wi9, PDBe:3wi9, PDBj:3wi9
PDBsum3wi9
PubMed24440558
UniProtQ5L1X8

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