Structure of PDB 6qq2 Chain A

Receptor sequence
>6qq2A (length=455) Species: 329 (Ralstonia pickettii) [Search protein sequence]
KLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQIS
EGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTG
PGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLIL
VEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLF
NGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEG
GTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAIL
KIDGAENKLVYSGKELDSVFLGDRAAPNMSAVTKATQASVSGTLTVQDQV
QAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGL
NGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVK
KVRAQ
3D structure
PDB6qq2 Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
ChainA
Resolution2.6 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) H91 D94 H96 H131 C132 H140 M145 H237 Q259 T260 H286
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 H94 C135 H143 M148 H91 C132 H140 M145
BS02 CU A H99 H134 H96 H131
BS03 NO2 A D97 H99 H134 D94 H96 H131
BS04 HEC A C364 C367 H368 P380 P381 L382 F387 I398 L403 N404 G405 S416 M418 M421 C361 C364 H365 P377 P378 L379 F384 I395 L400 N401 G402 S413 M415 M418
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:6qq2, PDBe:6qq2, PDBj:6qq2
PDBsum6qq2
PubMed32051772
UniProtI6NAW4

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