Structure of PDB 2y6e Chain F Binding Site BS01

Receptor Information
>2y6e Chain F (length=323) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HIQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPL
GMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQ
ELLAFLLDGLHEDLNRVKKKPLKDANGRPDAVVAKEAWENHRLRNDSVIV
DTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKTVALRDCIELFTTM
ETLQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSE
FVCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVS
LASEDQIVTKAAYVLFYQRRDDE
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2y6e Chain F Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2y6e The Dusp-Ubl Domain of Usp4 Enhances its Catalytic Efficiency by Promoting Ubiquitin Exchange.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		C461 C464
Binding residue
(residue number reindexed from 1)		C163 C166
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N306 C311 H881 D898
Catalytic site (residue number reindexed from 1) N11 C16 H278 D295
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
Biological Process
GO:0016579 protein deubiquitination

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:2y6e, PDBe:2y6e, PDBj:2y6e
PDBsum2y6e
PubMed25404403
UniProtQ13107|UBP4_HUMAN Ubiquitin carboxyl-terminal hydrolase 4 (Gene Name=USP4)

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