Structure of PDB 2hzh Chain A Binding Site BS02

Receptor Information
>2hzh Chain A (length=499) Species: 230624 (Trametes ochracea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AIGPSANLVVTNAAVAADGHSRDAVVVNGGTPGPLITGNKGDQFQLNVIN
NLTNFTMLKSTSVHWHGFFQKGTNWADGPAFVNQCPIAAGSSFLYDFSTP
IQAGTFWYHSHLSTQYCDGDRGPFVVYDPNDPSANLYDVDNLNTVITLTD
WYHTAAQNGPAKPGGADATLINGQGRGPSSPSADLAVISVTAGKRYRFRL
VSNSCDPNYTFSIDGHQMTIIQVDSINVQPLVVLKIQIYAAQRYSFILNA
NQAVNNYWIRANPNQGNVGFTNGINSAILRYSGAAATQPTTSQTSSVQPL
DQTNLHPLTATAVPGSPVAGGVNLAINQAFNFNGTNHFVDGASFVPPTVP
VLSQIVSGAQSAADLLASGLVYSLPSDANIEISFPATSAAAGGPHPFHLH
GHAFAVVRSAGSTTYNYNDPIFRDTVSTGTPAANDNVTIRFKTNNPGPWF
LHCHIDFHLEAGFAVVFAQDIPDVASANPTPNAWSDLCPVYDAASSSSQ
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain2hzh Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2hzh Crystal structure of laccase from Coriolus zonatus at 2.6 A resolution
Resolution2.6 Å
Binding residue
(original residue number in PDB)
H111 H400 H452
Binding residue
(residue number reindexed from 1)
H111 H400 H452
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H64 H66 H109 H111 H395 H398 H400 H452 C453 H454 I455 H458 F463
Catalytic site (residue number reindexed from 1) H64 H66 H109 H111 H395 H398 H400 H452 C453 H454 I455 H458 F463
Enzyme Commision number 1.10.3.2: laccase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0052716 hydroquinone:oxygen oxidoreductase activity
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Cellular Component
External links
PDB RCSB:2hzh, PDBe:2hzh, PDBj:2hzh
PDBsum2hzh
PubMed
UniProtQ8TG94

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