Research workbench
Papd-papk chaperone-pilus subunit complex from E.COLI P pilus
Analyse Papd-papk chaperone-pilus subunit complex from E.COLI P pilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PDK
- Type
- protein
- Length
- 364 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (chaperone protein papd); Protein (protein papk)
- UniProt
- P15319, P62532
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (chaperone protein papd) | protein | 215 | 8% helix, 51% strand | P15319 |
| B | Protein (protein papk) | protein | 149 | 9% helix, 40% strand | P62532 |
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 | 98 | 0.35 | 0.74 | 23 | empty |
| 2 | 74 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1624 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1PDK · Papd-papk chaperone-pilus subunit complex from E.COLI P pilus · the same entry in another collection · chain A against A, TM-score 1.00
- P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P62532 · AlphaFold monomer V2.0 prediction for fimbrial adapter papk (P62532) · a predicted model of the same protein · chain B against A, TM-score 0.84
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 P15319
- Every structure of UniProt P62532
- Elsewhere: RCSB PDB 1PDK · PDBe 1PDK · UniProt P15319 · UniProt P62532
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