Research workbench

DNA-binding domain from human RAP30, NMR, 30 structures

Analyse DNA-binding domain from human RAP30, NMR, 30 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BBY
Type: protein
Length: 69 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAP30
UniProt: P13984
Pockets: 1 · best druggability 0.28

Structure

solution nmr · 1 distinct chain · 51% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAP30	protein	69	51% helix, 7% strand	P13984

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	54	0.28	0.74	11	empty

Compared structures

2BBY · DNA-binding domain from human RAP30, NMR, 30 structures · the same entry in another collection · chain A against A, TM-score 1.00
P13984 · AlphaFold monomer V2.0 prediction for general transcription factor iif subunit 2 (P13984) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P13984
Elsewhere: RCSB PDB 2BBY · PDBe 2BBY · UniProt P13984

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