Structure of PDB 3qpk Chain A Binding Site BS07

Receptor Information
>3qpk Chain A (length=559) Species: 204285 (Melanocarpus albomyces) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPTCNTPSNRACWSDGFDINTDYEVSTPDTGVTQSYVFNLTEVDNWMGPD
GVVKEKVMLINGNIMGPNIVANWGDTVEVTVINNLVTNGTSIHWHGIHQK
DTNLHDGANGVTECPIPPKGGQRTYRWRARQYGTSWYHSHFSAQYGNGVV
GTIQINGPASLPYDIDLGVFPITDYYYRAADDLVHFTQNNAPPFSDNVLI
NGTAVNPNTGEGQYANVTLTPGKRHRLRILNTSTENHFQVSLVNHTMTVI
AADMVPVNAMTVDSLFLAVGQRYDVVIDASRAPDNYWFNVTFGGQAACGG
SLNPHPAAIFHYAGAPGGLPTDEGTPPVDHQCLDTLDVRPVVPRSVPVNS
FVKRPDNTLPVALDLTGTPLFVWKVNGSDINVDWGKPIIDYILTGNTSYP
VSDNIVQVDAVDQWTYWLIENDPEGPFSLPHPMHLHGHDFLVLGRSPDVP
AASQQRFVFDPAVDLARLNGDNPPRRDTTMLPAGGWLLLAFRTDNPGAWL
FHCHIAWHVSGGLSVDFLERPADLRQRISQEDEDDFNRVCDEWRAYWPTN
PYPKIDSGL
Ligand information
Ligand IDXE
InChIInChI=1S/Xe
InChIKeyFHNFHKCVQCLJFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Xe]
FormulaXe
NameXENON
ChEMBLCHEMBL1236802
DrugBankDB13453
ZINC
PDB chain3qpk Chain A Residue 576 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3qpk Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		V348 F351 Y416
Binding residue
(residue number reindexed from 1)		V348 F351 Y416
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H93 H95 H138 H140 H431 H434 H436 H502 C503 H504 I505 H508 L513
Catalytic site (residue number reindexed from 1) H93 H95 H138 H140 H431 H434 H436 H502 C503 H504 I505 H508 L513
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
Biological Process
GO:0030245 cellulose catabolic process
GO:0046274 lignin catabolic process
Cellular Component
GO:0043245 extraorganismal space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3qpk, PDBe:3qpk, PDBj:3qpk
PDBsum3qpk
PubMed21524088
UniProtQ70KY3|LAC1_MELAO Laccase-1 (Gene Name=LAC1)

[Back to BioLiP]