Research workbench
Structure of the tetrameric building block of the salmonella typhimurium prgi type three secretion system needle
Analyse Structure of the tetrameric building block of the salmonella typhimurium prgi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MEX
- Type
- protein
- Length
- 320 residues
- Chains
- 4
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein prgi
- UniProt
- P41784
- Pockets
- 8 · best druggability 0.69
Structure
solid-state nmr · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Protein prgi | protein | 80 | 79% helix, 0% strand | P41784 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.69 | 0.88 | 21 | empty |
| 2 | 94 | 0.62 | 0.88 | 21 | empty |
| 3 | 172 | 0.49 | 0.77 | 25 | empty |
| 4 | 159 | 0.49 | 0.77 | 19 | empty |
| 5 | 51 | 0.46 | 0.85 | 20 | empty |
Interfaces
5 interfaces between chains.
- B–D · 734 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 680 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 667 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 643 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 527 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2MEX · Structure of the tetrameric building block of the Salmonella Typhimurium PrgI Type three… · the same entry in another collection · chain A against A, TM-score 1.00
- P41784 · AlphaFold monomer V2.0 prediction for protein prgi (P41784) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P41784
- Elsewhere: RCSB PDB 2MEX · PDBe 2MEX · UniProt P41784
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