Structure of PDB 4lcd Chain A Binding Site BS01

Receptor Information
>4lcd Chain A (length=419) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYK
RDFRRKVIYFRSQPALRILPGQLHIKVRRKNIFEDAYQEIMRQTPEDLKK
RLMIKFDGYGGVSREFFFLLSHEMFNPFYGLFEYSAYDNYTIQINPNSGI
NPEHLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGV
DAEVYNSLNWMLENSIDGVLDLTFSADDERFGEVVTVDLKPDGRNIEVTD
GNKKEYVELYTQWRIVDRVQEQFKAFMDGFNELIPEDLVTVFDERELELL
IGGIAEIDIEDWKKHTDYRGYQESDEVIQWFWKAVSEWDNEQRARLLQFT
TGTSRIPVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYV
DYDSMKQKLTLAVEETIGF
Ligand information
>4lcd Chain C (length=8) Species: 559292 (Saccharomyces cerevisiae S288C) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
QPPAYDED
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 V406 D407 H408 K411 T412 T413
Binding residue
(residue number reindexed from 1)		Y22 V24 D25 H26 K29 T30 T31
Enzymatic activity
Catalytic site (original residue number in PDB) R461 E502 D563 H775 C777
Catalytic site (residue number reindexed from 1) R79 E115 D176 H388 C390
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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