MolNFT v1 · #139782 · protein
Structural basis of kindlin-mediated integrin recognition and activation
5XPZ · Fermitin family homolog 2: “Structural basis of kindlin-mediated integrin recognition and activation”. X-ray diffraction, 9 pockets (best druggability 0.76). MolNFT v1 #139782 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5XPZ
- Type
- protein
- Length
- 795 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fermitin family homolog 2
- UniProt
- Q8CIB5
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fermitin family homolog 2 | protein | 404 | 39% helix, 24% strand | Q8CIB5 |
| B | Fermitin family homolog 2 | protein | 391 | 36% helix, 23% strand | Q8CIB5 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 433 | 0.76 | 0.85 | 43 | GOL |
| 2 | 488 | 0.73 | 0.82 | 47 | empty |
| 3 | 61 | 0.51 | 0.86 | 16 | empty |
| 4 | 98 | 0.46 | 0.80 | 17 | empty |
| 5 | 59 | 0.42 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2413 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 5XPZ · 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 0.89
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 5XPZ · PDBe 5XPZ · UniProt Q8CIB5
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