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Crystal structure of human bfk

Analyse Crystal structure of human bfk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CCL
Type: protein
Length: 434 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BCL-2-like protein 15
UniProt: Q5TBC7
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 3 distinct chains · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-like protein 15	protein	141	79% helix, 0% strand	Q5TBC7
B	BCL-2-like protein 15	protein	146	74% helix, 0% strand	Q5TBC7
C	BCL-2-like protein 15	protein	147	76% helix, 0% strand	Q5TBC7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.53	0.79	19	empty
2	190	0.45	0.74	28	empty

Interfaces

2 interfaces between chains.

B–C · 357 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 198 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

7CCL · Crystal structure of human BFK · the same entry in another collection · chain A against A, TM-score 1.00
Q5TBC7 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 15 (Q5TBC7) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q5TBC7
Elsewhere: RCSB PDB 7CCL · PDBe 7CCL · UniProt Q5TBC7

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