Structure of PDB 2yqb Chain A

Receptor sequence
>2yqbA (length=454) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
KLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQIS
EGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMAHNIDLHGVTG
PGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLIL
VEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLF
NGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEG
GTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAIL
KIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQV
QAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGL
NGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVK
KVRA
3D structure
PDB2yqb Structures of protein-protein complexes involved in electron transfer.
ChainA
Resolution1.41 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 HEC A C364 C367 H368 P380 P381 L382 S385 F387 N404 G405 Y414 S416 M418 M421 C361 C364 H365 P377 P378 L379 S382 F384 N401 G402 Y411 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:2yqb, PDBe:2yqb, PDBj:2yqb
PDBsum2yqb
PubMed23535590
UniProtB2UHR8

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