Research workbench
Atomic structure of mycobacterium tuberculosis dppa
Analyse Atomic structure of mycobacterium tuberculosis dppa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E3D
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic dipeptide-binding lipoprotein dppa; Tetra-peptide picked up from the…
- UniProt
- A0A045KE34
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic dipeptide-binding lipoprotein dppa | protein | 510 | 35% helix, 21% strand | A0A045KE34 |
| B | Tetra-peptide picked up from the expression host | protein | 4 | 0% helix, 25% strand | — |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 229 | 0.81 | 0.94 | 46 | empty |
| 2 | 148 | 0.79 | 0.96 | 35 | empty |
| 3 | 239 | 0.59 | 0.80 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 426 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6E3D · Atomic structure of Mycobacterium tuberculosis DppA · 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 A0A045KE34
- Elsewhere: RCSB PDB 6E3D · PDBe 6E3D · UniProt A0A045KE34
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