Structure of PDB 3zbm Chain A

Receptor sequence
>3zbmA (length=455) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKAPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQVQ
AGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGLN
GKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVKK
VRAQP
3D structure
PDB3zbm Structures of protein-protein complexes involved in electron transfer.
ChainA
Resolution1.87 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 CU A H94 C135 H143 M148 H90 C131 H139 M144
BS02 CU A H99 H134 H95 H130
BS03 HEC A C364 C367 H368 P380 P381 L382 F387 N404 G405 S416 V417 M418 M421 C360 C363 H364 P376 P377 L378 F383 N400 G401 S412 V413 M414 M417
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:3zbm, PDBe:3zbm, PDBj:3zbm
PDBsum3zbm
PubMed23535590
UniProtB2UHR8

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