Research workbench
Crystal structure of the M42 aminopeptidase TMPEP1050 from thermotoga maritima
Analyse Crystal structure of the M42 aminopeptidase TMPEP1050 from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P6Y
- Type
- protein
- Length
- 3,964 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase
- EC
- 3.2.1.4
- UniProt
- Q9X0E0
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F | Aminopeptidase (EC 3.2.1.4) | protein | 331 | 30% helix, 29% strand | Q9X0E0 |
| B, E, G, H, I, J, K, L | Aminopeptidase (EC 3.2.1.4) | protein | 330 | 29% helix, 28% strand | Q9X0E0 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.77 | 0.87 | 30 | empty |
| 2 | 362 | 0.76 | 0.86 | 30 | empty |
| 3 | 349 | 0.75 | 0.86 | 30 | empty |
| 4 | 351 | 0.75 | 0.86 | 32 | empty |
| 5 | 1147 | 0.74 | 0.77 | 118 | empty |
Interfaces
44 interfaces between chains.
- E–G · 2184 Ų buried · 31 hydrogen bonds · protein-protein
- B–F · 2157 Ų buried · 25 hydrogen bonds · protein-protein
- H–J · 2141 Ų buried · 31 hydrogen bonds · protein-protein
- A–K · 2126 Ų buried · 28 hydrogen bonds · protein-protein
- I–L · 2126 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 4P6Y · Crystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritima · 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 Q9X0E0
- Elsewhere: RCSB PDB 4P6Y · PDBe 4P6Y · UniProt Q9X0E0
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