Structure of PDB 3zbm Chain A Binding Site BS01
Receptor Information
>3zbm Chain A (length=455) Species:
402626
(Ralstonia pickettii 12J) [
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LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKAPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQVQ
AGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGLN
GKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVKK
VRAQP
Ligand information
Ligand ID
CU
InChI
InChI=1S/Cu/q+2
InChIKey
JPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341
[Cu++]
Formula
Cu
Name
COPPER (II) ION
ChEMBL
DrugBank
DB14552
ZINC
PDB chain
3zbm Chain A Residue 1460 [
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Receptor-Ligand Complex Structure
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PDB
3zbm
Structures of protein-protein complexes involved in electron transfer.
Resolution
1.87 Å
Binding residue
(original residue number in PDB)
H94 C135 H143 M148
Binding residue
(residue number reindexed from 1)
H90 C131 H139 M144
Annotation score
1
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).
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
PDBsum
3zbm
PubMed
23535590
UniProt
B2UHR8
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