Structure of PDB 6qpt Chain B

Receptor sequence
>6qptB (length=319) Species: 329 (Ralstonia pickettii) [Search protein sequence]
PGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISEG
VSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGPG
GGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILVE
PPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFNG
AEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGGT
NVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILKI
DGAENKLVYSGKELDSVYL
3D structure
PDB6qpt Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H94 D97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
Catalytic site (residue number reindexed from 1) H89 D92 H94 H129 C130 H138 M143 H235 Q257 T258 H284
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 B H94 C135 H143 M148 H89 C130 H138 M143
BS02 CU B H99 H134 H94 H129
BS03 NO2 B D97 H134 D92 H129
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0050421 nitrite reductase (NO-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:6qpt, PDBe:6qpt, PDBj:6qpt
PDBsum6qpt
PubMed32051772
UniProtI6NAW4

[Back to BioLiP]