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MolNFT v1 · #51209 · protein

FCHO2 F-bar domain

2V0O · Fch domain only protein 2: “FCHO2 F-bar domain”. X-ray diffraction, 12 pockets (best druggability 0.75). MolNFT v1 #51209 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
2V0O
Type
protein
Length
816 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fch domain only protein 2
UniProt
Q96CF5
Pockets
12 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 85% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFch domain only protein 2protein27385% helix, 1% strandQ96CF5
BFch domain only protein 2protein27184% helix, 1% strandQ96CF5
CFch domain only protein 2protein27285% helix, 0% strandQ96CF5

Ligands and binding sites

  • ACT · Acetate ion · additive · 3 copies · chains A, B, C

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.750.9822empty
2590.740.9917ACT
3530.720.9816ACT
47830.710.7770empty
55650.660.7746empty

Interfaces

3 interfaces between chains.

  • A–B · 4799 Ų buried · 40 hydrogen bonds · protein-protein
  • A–C · 949 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 127 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2V0O · FCHO2 F-BAR domain · the same entry in another collection · chain A against A, TM-score 1.00

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