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The solution structure of RAP1 brct domain from saccharomyces cerevisiae

Analyse The solution structure of RAP1 brct domain from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L42
Type: protein
Length: 97 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA-binding protein RAP1
UniProt: P11938
Pockets: 2 · best druggability 0.49

Structure

solution nmr · 1 distinct chain · 21% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-binding protein RAP1	protein	97	21% helix, 8% strand	P11938

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.49	0.78	29	empty
2	142	0.48	0.78	32	empty

Compared structures

2L42 · The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P11938 · AlphaFold monomer V2.0 prediction for DNA-binding protein RAP1 (P11938) · a predicted model of the same protein · chain A against A, TM-score 0.49

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 P11938
Elsewhere: RCSB PDB 2L42 · PDBe 2L42 · UniProt P11938

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