MolNFT v1 · #16701 · protein
Internalin (inla, listeria monocytogenes) - functional domain, uncomplexed
1O6V · Internalin a: “Internalin (inla, listeria monocytogenes) - functional domain, uncomplexed”. X-ray diffraction, 1 ligand (CA). MolNFT v1 #16701 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1O6V
- Type
- protein
- Length
- 922 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Internalin a
- UniProt
- P25146
- Ligands
- CA
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Internalin a | protein | 462 | 16% helix, 24% strand | P25146 |
| B | Internalin a | protein | 460 | 16% helix, 24% strand | P25146 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 194 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1O6V · Internalin (INLA, Listeria monocytogenes) - functional domain, uncomplexed · the same entry in another collection · chain A against A, TM-score 1.00
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 P25146
- Elsewhere: RCSB PDB 1O6V · PDBe 1O6V · UniProt P25146
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