Structure of PDB 3tb3 Chain B Binding Site BS01

Receptor Information
>3tb3 Chain B (length=204) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLF
KWQPGEEPAGSVVQDSRLDTIFFAKQVINNAAATQAIVSVLLNCTHQDVH
LGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARAFHFVSYVPVN
GRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMA
IVSD
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain3tb3 Chain B Residue 229 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3tb3 Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains.
Resolution2.3 Å
Binding residue
(original residue number in PDB)
E109 E113
Binding residue
(residue number reindexed from 1)
E103 E107
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) Q82 A88 H164 D179
Catalytic site (residue number reindexed from 1) Q76 A82 H142 D157
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
GO:0070628 proteasome binding
Biological Process
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0016579 protein deubiquitination
Cellular Component
GO:0031011 Ino80 complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3tb3, PDBe:3tb3, PDBj:3tb3
PDBsum3tb3
PubMed21851340
UniProtQ9Y5K5|UCHL5_HUMAN Ubiquitin carboxyl-terminal hydrolase isozyme L5 (Gene Name=UCHL5)

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