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Crystal structure of human dipeptidyl peptidase III
Analyse Crystal structure of human dipeptidyl peptidase III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FVY
- Type
- protein
- Length
- 718 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl-peptidase 3
- EC
- 3.4.14.4
- UniProt
- Q9NY33
- Ligands
- MG, ZN, CL
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dipeptidyl-peptidase 3 (EC 3.4.14.4) | protein | 718 | 51% helix, 15% strand | Q9NY33 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1158 | 0.81 | 0.82 | 128 | MG |
| 2 | 78 | 0.41 | 0.79 | 24 | empty |
| 3 | 57 | 0.29 | 0.75 | 18 | empty |
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 Q9NY33
- Elsewhere: RCSB PDB 3FVY · PDBe 3FVY · UniProt Q9NY33
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