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MolNFT v1 · #135460 · protein

Crystal structure of FPV039:BMF BH3 complex

5TZQ · BCL-2-like protein FPV039: “Crystal structure of FPV039:BMF BH3 complex”. X-ray diffraction, 2 pockets (best druggability 0.57). MolNFT v1 #135460 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5TZQ
Type
protein
Length
306 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BCL-2-like protein FPV039; BCL-2-modifying factor
UniProt
Q9J5G4, A9XRG9
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 4 distinct chains · 80% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABCL-2-like protein FPV039protein13279% helix, 0% strandQ9J5G4
BBCL-2-like protein FPV039protein13078% helix, 0% strandQ9J5G4
CBCL-2-modifying factorprotein2286% helix, 0% strandA9XRG9
DBCL-2-modifying factorprotein2291% helix, 0% strandA9XRG9

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.570.8028EDO
2750.330.7515empty

Interfaces

3 interfaces between chains.

  • B–C · 924 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 890 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 774 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5TZQ · Crystal Structure of FPV039:Bmf BH3 complex · the same entry in another collection · chain A against A, TM-score 1.00

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