Structure of PDB 4ax3 Chain D

Receptor sequence
>4ax3D (length=457) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
SAKLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQ
ISEGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGV
TGPGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGL
ILVEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYV
LFNGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRY
EGGTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMA
ILKIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQD
QVQAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLH
GLNGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAED
VKKVRAQ
3D structure
PDB4ax3 Structures of protein-protein complexes involved in electron transfer.
ChainD
Resolution1.6 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) H93 D96 H98 H133 C134 H142 M147 H239 Q261 T262 H288
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 D H94 C135 H143 M148 H93 C134 H142 M147
BS02 CU D H99 H134 H98 H133
BS03 HEC D C364 C367 H368 P380 P381 L382 S385 F387 N404 G405 S416 M418 M421 C363 C366 H367 P379 P380 L381 S384 F386 N403 G404 S415 M417 M420
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

View graph for
Cellular Component
External links
PDB RCSB:4ax3, PDBe:4ax3, PDBj:4ax3
PDBsum4ax3
PubMed23535590
UniProtB2UHR8

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