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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: 2MCN
Type: protein
Length: 133 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: NOT
Source: Homo sapiens; Mus musculus
Molecule: CD2-associated protein; Ubiquitin
UniProt: Q9JLQ0, P0CG48

Structure

solution nmr · resolution NOT · 2 distinct chains · 14% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CD2-associated protein	protein	57	5% helix, 49% strand	Q9JLQ0
B	Ubiquitin	protein	76	21% helix, 29% strand	P0CG48

Interfaces

1 interface between chains.

A–B · 832 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

2MCN · 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 A against A, TM-score 0.94
P0CG48 · AlphaFold monomer V2.0 prediction for polyubiquitin-C (P0CG48) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 Q9JLQ0
Every structure of UniProt P0CG48
Elsewhere: RCSB PDB 2MCN · PDBe 2MCN · UniProt Q9JLQ0 · UniProt P0CG48

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