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Atypical polyproline recognition by the cms N-terminal SH3 domain. CMS:CD2 heterotrimer

Analyse Atypical polyproline recognition by the cms N-terminal SH3 domain. CMS:CD2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J6O
Type: protein
Length: 64 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CD2-associated protein; T-cell surface antigen CD2
UniProt: Q9Y5K6, P06729

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CD2-associated protein	protein	57	5% helix, 49% strand	Q9Y5K6
C	T-cell surface antigen CD2	protein	7	0% helix, 0% strand	P06729

Interfaces

1 interface between chains.

A–C · 407 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2J6O · Atypical polyproline recognition by the cms N-terminal SH3 domain. CMS:CD2 heterotrimer · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y5K6 · AlphaFold monomer V2.0 prediction for CD2-associated protein (Q9Y5K6) · a predicted model of the same protein · chain A against A, TM-score 0.98
P06729 · AlphaFold monomer V2.0 prediction for T-cell surface antigen CD2 (P06729) · a predicted model of the same protein · chain C against A, TM-score 0.60

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 Q9Y5K6
Every structure of UniProt P06729
Elsewhere: RCSB PDB 2J6O · PDBe 2J6O · UniProt Q9Y5K6 · UniProt P06729

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