Structure of PDB 6qpt Chain E

Receptor sequence
>6qptE (length=320) Species: 329 (Ralstonia pickettii) [Search protein sequence]
LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVYL
3D structure
PDB6qpt Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
ChainE
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) H90 D93 H95 H130 C131 H139 M144 H236 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 NO2 E H240 I242 H289 H236 I238 H285
BS02 CU E H94 C135 H143 M148 H90 C131 H139 M144
BS03 CU E H99 H134 H95 H130
BS04 NO2 E D97 H99 H134 D93 H95 H130
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

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