Structure of PDB 4ax3 Chain A

Receptor sequence
>4ax3A (length=456) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
AKLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQI
SEGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVT
GPGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLI
LVEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVL
FNGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYE
GGTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAI
LKIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQ
VQAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHG
LNGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDV
KKVRAQ
3D structure
PDB4ax3 Structures of protein-protein complexes involved in electron transfer.
ChainA
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) H92 D95 H97 H132 C133 H141 M146 H238 Q260 T261 H287
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 H92 C133 H141 M146
BS02 CU A H99 H134 H97 H132
BS03 HEC A C364 C367 H368 P380 P381 L382 S385 F387 L403 N404 G405 I407 S416 M418 M421 C362 C365 H366 P378 P379 L380 S383 F385 L401 N402 G403 I405 S414 M416 M419
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:4ax3, PDBe:4ax3, PDBj:4ax3
PDBsum4ax3
PubMed23535590
UniProtB2UHR8

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