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Crystal structure of the dbl-homology domain of BCR-abl in complex with monobody MB(BCR-DH_4).

Analyse Crystal structure of the dbl-homology domain of BCR-abl in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5N7E
Type: protein
Length: 279 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MB(BCR-DH_4); Breakpoint cluster region protein
EC: 2.7.11.1
UniProt: P11274
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MB(BCR-DH_4)	protein	93	0% helix, 53% strand	—
B	Breakpoint cluster region protein (EC 2.7.11.1)	protein	186	77% helix, 0% strand	P11274

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	267	0.72	0.86	37	empty

Interfaces

1 interface between chains.

A–B · 432 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5N7E · Crystal structure of the Dbl-homology domain of Bcr-Abl in complex with monobody… · the same entry in another collection · chain A against A, TM-score 1.00
P11274 · AlphaFold monomer V2.0 prediction for breakpoint cluster region protein (P11274) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P11274
Elsewhere: RCSB PDB 5N7E · PDBe 5N7E · UniProt P11274

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