Research workbench
Crystal structure of haemophilus influenzae oppa complex with endogenous peptide
Analyse Crystal structure of haemophilus influenzae oppa complex with endogenous peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DQQ
- Type
- protein
- Length
- 525 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic oligopeptide-binding protein; Ala-ala-ala-ala
- UniProt
- Q4QLH0
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic oligopeptide-binding protein | protein | 521 | 34% helix, 22% strand | Q4QLH0 |
| B | Ala-ala-ala-ala | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.79 | 0.98 | 30 | empty |
| 2 | 120 | 0.43 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 383 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6DQQ · Crystal structure of Haemophilus influenzae OppA complex with endogenous peptide · 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 Q4QLH0
- Elsewhere: RCSB PDB 6DQQ · PDBe 6DQQ · UniProt Q4QLH0
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