MolNFT v1 · #125369 · protein
Crystal structure of D62A mutant of thermotoga maritima TMPEP1050 aminopeptidase
5L6Z · Leucylaminopeptidase: “Crystal structure of D62A mutant of thermotoga maritima TMPEP1050 aminopeptidase”. X-ray diffraction, 1 ligand (NA), 4 pockets (best druggability 0.42). MolNFT v1 #125369 on GenesisL1: 3D structure, binding…
- PDB
- 5L6Z
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucylaminopeptidase
- EC
- 3.2.1.4
- UniProt
- Q9X0E0
- Ligands
- NA
- Pockets
- 4 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucylaminopeptidase (EC 3.2.1.4) | protein | 310 | 30% helix, 30% strand | Q9X0E0 |
| B | Leucylaminopeptidase (EC 3.2.1.4) | protein | 313 | 28% helix, 30% strand | Q9X0E0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.42 | 0.78 | 20 | empty |
| 2 | 101 | 0.41 | 0.77 | 19 | empty |
| 3 | 82 | 0.39 | 0.78 | 22 | empty |
| 4 | 55 | 0.34 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 749 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5L6Z · Crystal structure of D62A mutant of Thermotoga maritima TmPEP1050 aminopeptidase · 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 5L6Z · PDBe 5L6Z · UniProt Q9X0E0
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