Structure of PDB 3pps Chain C Binding Site BS02

Receptor Information
>3pps Chain C (length=564) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGPTCNTPSNRACWTNGFDINTDYEVSTPNTGRTVAYQLTLTEKENWIGP
DGVLKNVVMLVNDKIIGPTIRANWGDNIEVTVINNLKTNGTSMHWHGLRQ
LGNVFNDGANGVTECPIPPKGGRKTYKFRATQYGTSWYHSHFSAQYGNGV
VGTIQIDGPASLPYDIDLGVFPLMDYYYRSADELVHFTQSNGAPPSDNVL
FNGTARHPETGAGQWYNVTLTPGKRHRLRIINTSTDNHFQVSLVGHNMTV
IATDMVPVNAFTVSSLFLAVGQRYDVTIDANSPVGNYWFNVTFGDGLCGS
SNNKFPAAIFRYQGAPATLPTDQGLPVPNHMCLDNLNLTPVVTRSAPVNN
FVKRPSNTLGVTLDIGGTPLFVWKVNGSAINVDWGKPILDYVMSGNTSYP
VSDNIVQVDAVDQWTYWLIENDPTNPIVSLPHPMHLHGHDFLVLGRSPDE
LPSAGVRHIFDPAKDLPRLKGNNPVRRDVTMLPAGGWLLLAFKTDNPGAW
LFHCHIAWHVSGGLSVDFLERPNDLRTQLNSNAKRADRDDFNRVCREWNA
YWPTNPFPKIDSGL
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 chain3pps Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3pps Crystal structure of an ascomycete fungal laccase from Thielavia arenaria--common structural features of asco-laccases.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		H141 H437 H503
Binding residue
(residue number reindexed from 1)		H141 H437 H503
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H94 H96 H139 H141 H432 H435 H437 H503 C504 H505 I506 H509 L514
Catalytic site (residue number reindexed from 1) H94 H96 H139 H141 H432 H435 H437 H503 C504 H505 I506 H509 L514
Enzyme Commision number 1.10.3.2: laccase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:3pps, PDBe:3pps, PDBj:3pps
PDBsum3pps
PubMed21535408
UniProtF6N9E7

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