Research workbench
NMR structure of E. COLI trigger factor in complex with unfolded PHOA220-310
Analyse NMR structure of E. COLI trigger factor in complex with unfolded PHOA220-310 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MLX
- Type
- protein
- Length
- 523 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trigger factor; Alkaline phosphatase
- EC
- 5.2.1.8
- UniProt
- U6N325, U6N3P1
- Pockets
- 6 · best druggability 0.77
Structure
solution nmr · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trigger factor (EC 5.2.1.8) | protein | 432 | 47% helix, 22% strand | U6N325 |
| B | Alkaline phosphatase | protein | 91 | 8% helix, 0% strand | U6N3P1 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.77 | 0.95 | 20 | empty |
| 2 | 544 | 0.63 | 0.75 | 53 | empty |
| 3 | 124 | 0.62 | 0.85 | 23 | empty |
| 4 | 93 | 0.37 | 0.76 | 16 | empty |
| 5 | 61 | 0.35 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3136 Ų buried · 73 hydrogen bonds · protein-protein
Compared structures
- 2MLX · NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310 · 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 U6N325
- Every structure of UniProt U6N3P1
- Elsewhere: RCSB PDB 2MLX · PDBe 2MLX · UniProt U6N325 · UniProt U6N3P1
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