MolNFT v1 · #14206 · protein
An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11B a-domain
1M1U · Integrin alpha-M: “An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11B a-domain”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #14206 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1M1U
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrin alpha-M
- UniProt
- P11215
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrin alpha-M | protein | 184 | 41% helix, 23% strand | P11215 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1M1U · An isoleucine-based allosteric switch controls affinity and shape shifting in integrin… · the same entry in another collection · chain A against A, TM-score 1.00
- P11215 · AlphaFold monomer V2.0 prediction for integrin alpha-M (P11215) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P11215
- Elsewhere: RCSB PDB 1M1U · PDBe 1M1U · UniProt P11215
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