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BioLiP

Structure of PDB 4lcd Chain B

Receptor sequence
>4lcdB (length=413) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKR
DFRRKVIYFRSQPALRILPGQLHIKVRRKNIFEDAYQEIMRQTPEDLKKR
LMIKFDGGGVSREFFFLLSHEMFNPFYGLFEYSAYDNYTIQINPNSGINP
EHLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGVDA
EVYNSLNWMLENSIDLTFSADDERFGEVVTVDLKPDGRNIEVTDGNKKEY
VELYTQWRIVDRVQEQFKAFMDGFNELIPEDLVTVFDERELELLIGGIAE
IDIEDWKKHTDYRGYQESDEVIQWFWKAVSEWDNEQRARLLQFTTGTSRI
PVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYVDYDSMK
QKLTLAVEETIGF
3D structure
PDB4lcd Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B Y404 H408 K411 T412 T413 W415 Y21 H25 K28 T29 T30 W32
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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