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Crystal structure of the dh domain of FARP2

Analyse Crystal structure of the dh domain of FARP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GYV
Type: protein
Length: 1,941 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferm, rhogef and pleckstrin domain-containing protein 2
UniProt: Q91VS8
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, F, H	Ferm, rhogef and pleckstrin domain-containing protein 2	protein	216	79% helix, 0% strand	Q91VS8
E, G, I	Ferm, rhogef and pleckstrin domain-containing protein 2	protein	215	78% helix, 0% strand	Q91VS8

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	773	0.76	0.81	63	empty
2	780	0.76	0.81	61	empty
3	707	0.76	0.81	53	empty
4	56	0.71	0.98	12	empty
5	51	0.70	0.98	12	empty

Interfaces

12 interfaces between chains.

B–C · 1889 Å² buried · 19 hydrogen bonds · protein-protein
F–G · 1600 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 1560 Å² buried · 18 hydrogen bonds · protein-protein
H–I · 1555 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 789 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 modified (engineered).

Compared structures

4GYV · Crystal structure of the DH domain of FARP2 · the same entry in another collection · chain I against I, TM-score 1.00
Q91VS8 · AlphaFold monomer V2.0 prediction for ferm, arhgef and pleckstrin domain-containing… · a predicted model of the same protein · chain I against A, TM-score 0.97

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 Q91VS8
Elsewhere: RCSB PDB 4GYV · PDBe 4GYV · UniProt Q91VS8

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