Structure of PDB 2zoo Chain A Binding Site BS02
Receptor Information
>2zoo Chain A (length=438) Species:
326442
(Pseudoalteromonas translucida TAC125) [
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LKTEQAILTPPPMVPPAINRDHSAKVVINLETREQVGRIADGVEYVFWSF
GETVPGSFIRVREGDEIEFNLSNHPSSKMPHNIDLHAVTGPGGGAESSFT
APGHTSTFNFKALNPGLYIYHCATAPVGMHIANGMYGLILVEPKEGLAPV
DREYYLVQGDFYTKGEFGEAGLQPFDMAKAIDEDADYVVFNGSVGSTTDE
NSLTAKVGETVRLYIGNGGPNLVSSFHVIGEIFDTVYVEGGSLKNHNVQT
TLIPAGGAAIVEFKVEVPGTFILVDHSIFRAFNKGALAMLKVEGPDDHSI
FTGKTAENVYLPEGSAIQSLDNTFTKITANNKDEQIRFGQRVYEANCMAC
HQANGEGIPGAFPPLAKSDYLNNNPLLGVNAIIKGLSGPIKVNNVNYNGV
MPAMNLNDEDIANVITFVLNNWDNAGGKVSAEQVAKQR
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
2zoo Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
2zoo
Electron transfer processes within and between proteins containing the HEME C and blue Cu
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
H89 H124
Binding residue
(residue number reindexed from 1)
H86 H121
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H84 D87 H89 H124 C125 H133 M138 H230 Q252 T253 H279
Catalytic site (residue number reindexed from 1)
H81 D84 H86 H121 C122 H130 M135 H227 Q249 T250 H276
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
Biological Process
GO:0019333
denitrification pathway
GO:0042128
nitrate assimilation
Cellular Component
GO:0042597
periplasmic space
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2zoo
,
PDBe:2zoo
,
PDBj:2zoo
PDBsum
2zoo
PubMed
UniProt
Q3IGF7
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