Research workbench
Cryo-EM structure of the human pathogen mycoplasma pneumoniae P1
Analyse Cryo-EM structure of the human pathogen mycoplasma pneumoniae P1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BWM
- Type
- protein
- Length
- 1,219 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adhesin P1
- UniProt
- P11311
- Pockets
- 18 · best druggability 0.76
Structure
electron microscopy · 1 distinct chain · 19% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adhesin P1 | protein | 1219 | 19% helix, 19% strand | P11311 |
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1009 | 0.76 | 0.79 | 84 | empty |
| 2 | 458 | 0.69 | 0.80 | 34 | empty |
| 3 | 53 | 0.65 | 0.95 | 17 | empty |
| 4 | 280 | 0.64 | 0.81 | 39 | empty |
| 5 | 365 | 0.64 | 0.79 | 30 | empty |
Compared structures
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 P11311
- Elsewhere: RCSB PDB 7BWM · PDBe 7BWM · UniProt P11311
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