Research workbench
Structure of 299-452 fragment of the USPA1 protein from moraxella catarrhalis
Analyse Structure of 299-452 fragment of the USPA1 protein from moraxella catarrhalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QP4
- Type
- protein
- Length
- 467 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- USPA1
- UniProt
- Q9XD56
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | USPA1 | protein | 157 | 76% helix, 8% strand | Q9XD56 |
| B, C | USPA1 | protein | 155 | 75% helix, 8% strand | Q9XD56 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, C, B
- CL · Chloride ion · ion · 4 copies · chains A, B, C
- HEZ · Hexane-1,6-diol · additive · 12 copies · chains A, B, C
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 | 82 | 0.50 | 0.83 | 14 | empty |
| 2 | 59 | 0.37 | 0.79 | 15 | HEZ |
Interfaces
3 interfaces between chains.
- B–C · 3315 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 3265 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 3201 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 6QP4 · Structure of 299-452 fragment of the UspA1 protein from Moraxella catarrhalis · 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 Q9XD56
- Elsewhere: RCSB PDB 6QP4 · PDBe 6QP4 · UniProt Q9XD56
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