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BioLiP

Structure of PDB 4lcd Chain B Binding Site BS01

Receptor Information
>4lcd Chain B (length=413) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKR
DFRRKVIYFRSQPALRILPGQLHIKVRRKNIFEDAYQEIMRQTPEDLKKR
LMIKFDGGGVSREFFFLLSHEMFNPFYGLFEYSAYDNYTIQINPNSGINP
EHLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGVDA
EVYNSLNWMLENSIDLTFSADDERFGEVVTVDLKPDGRNIEVTDGNKKEY
VELYTQWRIVDRVQEQFKAFMDGFNELIPEDLVTVFDERELELLIGGIAE
IDIEDWKKHTDYRGYQESDEVIQWFWKAVSEWDNEQRARLLQFTTGTSRI
PVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYVDYDSMK
QKLTLAVEETIGF
Ligand information
>4lcd Chain D (length=14) Species: 559292 (Saccharomyces cerevisiae S288C) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
AQPPAYDEDDEAGA
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4lcd Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		Y404 H408 K411 T412 T413 W415
Binding residue
(residue number reindexed from 1)		Y21 H25 K28 T29 T30 W32
Enzymatic activity
Catalytic site (original residue number in PDB) R461 E502 D563 H775 C777
Catalytic site (residue number reindexed from 1) R78 E113 D174 H382 C384
Enzyme Commision number 2.3.2.26: HECT-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0004842 ubiquitin-protein transferase activity

View graph for
Molecular Function
External links
PDB RCSB:4lcd, PDBe:4lcd, PDBj:4lcd
PDBsum4lcd
PubMed23936628
UniProtP39940|RSP5_YEAST E3 ubiquitin-protein ligase RSP5 (Gene Name=RSP5)

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