MolNFT v1 · #52204 · protein

Vaccinia virus anti-apoptotic F1L is a novel BCL-2-like domain swapped dimer

2VTY · Protein F1: “Vaccinia virus anti-apoptotic F1L is a novel BCL-2-like domain swapped dimer”. X-ray diffraction, 2 pockets (best druggability 0.46). MolNFT v1 #52204 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2VTY
Type: protein
Length: 144 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein F1
UniProt: O57173
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein F1	protein	144	80% helix, 0% strand	O57173

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	203	0.46	0.73	22	empty
2	151	0.41	0.73	18	empty

Compared structures

2VTY · Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain swapped dimer · the same entry in another collection · chain A against A, TM-score 1.00

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 O57173
Elsewhere: RCSB PDB 2VTY · PDBe 2VTY · UniProt O57173

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