Research workbench
Crystal structure of a 3:1 complex of treponema pallidum TATP(T) (TP0957) bound to tatt (TP0956)
Analyse Crystal structure of a 3:1 complex of treponema pallidum TATP(T) (TP0957) bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DI4
- Type
- protein
- Length
- 573 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tatt (TP0956); TATP(T) (TP0957)
- UniProt
- O83922, O83923
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tatt (TP0956) | protein | 273 | 75% helix, 0% strand | O83922 |
| B | TATP(T) (TP0957) | protein | 300 | 49% helix, 18% strand | O83923 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1148 | 0.84 | 0.84 | 96 | PG4 |
| 2 | 645 | 0.75 | 0.81 | 71 | empty |
| 3 | 71 | 0.61 | 0.90 | 20 | empty |
| 4 | 207 | 0.53 | 0.77 | 30 | PGE |
| 5 | 79 | 0.44 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1094 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4DI4 · Crystal structure of a 3:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT… · the same entry in another collection · chain A against A, TM-score 1.00
- O83922 · AlphaFold monomer V2.0 prediction for uncharacterized protein TP_0956 (O83922) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O83922
- Every structure of UniProt O83923
- Elsewhere: RCSB PDB 4DI4 · PDBe 4DI4 · UniProt O83922 · UniProt O83923
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