Research workbench
Activated conformation of integrin ALPHA1 I-domain mutant
Analyse Activated conformation of integrin ALPHA1 I-domain mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A0Q
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrin alpha-1
- UniProt
- P56199
- Ligands
- MG
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrin alpha-1 | protein | 187 | 42% helix, 22% strand | P56199 |
| B | Integrin alpha-1 | protein | 192 | 41% helix, 21% strand | P56199 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.40 | 0.75 | 22 | MG |
| 2 | 130 | 0.37 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 206 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P56199
- Elsewhere: RCSB PDB 4A0Q · PDBe 4A0Q · UniProt P56199
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