MolNFT v1 · #17187 · protein
The structural basis of multispecificity in the oligopeptide-binding protein oppa
1OLA · Oligo-peptide binding protein: “The structural basis of multispecificity in the oligopeptide-binding protein oppa”. X-ray diffraction, 1 ligand (IUM), 2 pockets (best druggability 0.42). MolNFT v1 #17187 on GenesisL1: 3D structure…
- PDB
- 1OLA
- Type
- protein
- Length
- 521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oligo-peptide binding protein; Peptide val-lys-pro-gly
- UniProt
- P06202
- Ligands
- IUM
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligo-peptide binding protein | protein | 517 | 35% helix, 22% strand | P06202 |
| B | Peptide val-lys-pro-gly | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- IUM · Uranyl (VI) ion · metal · 2 copies · chains A
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 | 109 | 0.42 | 0.77 | 19 | empty |
| 2 | 77 | 0.35 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 477 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1OLA · The structural basis of multispecificity in the oligopeptide-binding protein oppa · the same entry in another collection · chain A against A, TM-score 1.00
- P06202 · AlphaFold monomer V2.0 prediction for periplasmic oligopeptide- binding protein (P06202) · a predicted model of the same protein · 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 P06202
- Elsewhere: RCSB PDB 1OLA · PDBe 1OLA · UniProt P06202
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