Structure of PDB 4lcd Chain A

Receptor sequence
>4lcdA (length=419) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
VSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYK
RDFRRKVIYFRSQPALRILPGQLHIKVRRKNIFEDAYQEIMRQTPEDLKK
RLMIKFDGYGGVSREFFFLLSHEMFNPFYGLFEYSAYDNYTIQINPNSGI
NPEHLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGV
DAEVYNSLNWMLENSIDGVLDLTFSADDERFGEVVTVDLKPDGRNIEVTD
GNKKEYVELYTQWRIVDRVQEQFKAFMDGFNELIPEDLVTVFDERELELL
IGGIAEIDIEDWKKHTDYRGYQESDEVIQWFWKAVSEWDNEQRARLLQFT
TGTSRIPVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYV
DYDSMKQKLTLAVEETIGF
3D structure
PDB4lcd Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3.
ChainA
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 A Y404 V406 D407 H408 K411 T412 T413 Y22 V24 D25 H26 K29 T30 T31
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)

[Back to BioLiP]