Research workbench

Structural basis of kindlin-mediated integrin recognition and activation

Analyse Structural basis of kindlin-mediated integrin recognition and activation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XPY
Type: protein
Length: 454 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fermitin family homolog 2
UniProt: Q8CIB5
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fermitin family homolog 2	protein	454	34% helix, 22% strand	Q8CIB5

Ligands and binding sites

ACT · Acetate ion · additive · 5 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	578	0.77	0.83	48	ACT
2	87	0.55	0.85	19	ACT
3	145	0.46	0.77	22	empty
4	105	0.41	0.77	19	empty
5	65	0.37	0.78	17	empty

Compared structures

5XPY · Structural basis of kindlin-mediated integrin recognition and activation · the same entry in another collection · chain A against A, TM-score 1.00
Q8CIB5 · AlphaFold monomer V2.0 prediction for fermitin family homolog 2 (Q8CIB5) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q8CIB5
Elsewhere: RCSB PDB 5XPY · PDBe 5XPY · UniProt Q8CIB5

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