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Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications

Analyse Distinct ubiquitin binding modes exhibited by SH3 domains: molecular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LZ6
Type: protein
Length: 136 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin; CD2-associated protein
UniProt: P0CG48, Q9JLQ0
Pockets: 1 · best druggability 0.42

Structure

solution nmr · 2 distinct chains · 9% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin	protein	76	16% helix, 32% strand	P0CG48
B	CD2-associated protein	protein	60	0% helix, 45% strand	Q9JLQ0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.42	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 604 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2LZ6 · Distinct ubiquitin binding modes exhibited by sh3 domains: molecular determinants and… · the same entry in another collection · chain A against A, TM-score 1.00
Q9JLQ0 · AlphaFold monomer V2.0 prediction for CD2-associated protein (Q9JLQ0) · a predicted model of the same protein · chain B against A, TM-score 0.87

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0CG48
Every structure of UniProt Q9JLQ0
Elsewhere: RCSB PDB 2LZ6 · PDBe 2LZ6 · UniProt P0CG48 · UniProt Q9JLQ0

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