Research workbench

Crystal structure of selenomethionine-derived human bfk

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

PDB: 7CCM
Type: protein
Length: 435 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 0.55

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BCL-2-like protein 15	protein	141	77% helix, 0% strand	Q5TBC7
B, C	BCL-2-like protein 15	protein	147	77% 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	205	0.55	0.79	20	empty
2	181	0.47	0.76	26	empty

Interfaces

2 interfaces between chains.

B–C · 386 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 217 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 modified (engineered).

Compared structures

7CCM · Crystal structure of selenomethionine-derived 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 7CCM · PDBe 7CCM · UniProt Q5TBC7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.