MolNFT v1 · #117727 · protein
Structure of ligand free human DPP3 in closed form.
5EGY · Dipeptidyl peptidase 3: “Structure of ligand free human DPP3 in closed form.”. X-ray diffraction, 2 ligands (ZN, MG), 4 pockets (best druggability 0.88). MolNFT v1 #117727 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5EGY
- Type
- protein
- Length
- 724 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
- ZN, MG
- Pockets
- 4 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dipeptidyl peptidase 3 (EC 3.4.14.4) | protein | 724 | 48% helix, 16% strand | Q9NY33 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.88 | 0.91 | 119 | ZN |
| 2 | 126 | 0.68 | 0.90 | 31 | empty |
| 3 | 85 | 0.43 | 0.79 | 25 | MG |
| 4 | 52 | 0.24 | 0.73 | 13 | 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 5EGY · PDBe 5EGY · UniProt Q9NY33
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