MolNFT v1 · #126250 · protein
Cys-gly dipeptidase glij mutant D38H
5LX4: “Cys-gly dipeptidase glij mutant D38H”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.36). MolNFT v1 #126250 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LX4
- Type
- protein
- Length
- 381 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidase
- EC
- 3.4.13.19
- UniProt
- Q4WMJ8
- Ligands
- FE
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dipeptidase (EC 3.4.13.19) | protein | 381 | 51% helix, 12% strand | Q4WMJ8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.36 | 0.73 | 15 | empty |
| 2 | 63 | 0.34 | 0.77 | 13 | empty |
| 3 | 73 | 0.31 | 0.73 | 19 | FE |
Compared structures
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 Q4WMJ8
- Elsewhere: RCSB PDB 5LX4 · PDBe 5LX4 · UniProt Q4WMJ8
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