MolNFT v1 · #21255 · protein
Crystal structure of human thimet oligopeptidase.
1S4B: “Crystal structure of human thimet oligopeptidase.”. X-ray diffraction, 1 ligand (ZN), 6 pockets (best druggability 0.76). MolNFT v1 #21255 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1S4B
- Type
- protein
- Length
- 654 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thimet oligopeptidase
- EC
- 3.4.24.15
- UniProt
- P52888
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Thimet oligopeptidase (EC 3.4.24.15) | protein | 654 | 60% helix, 8% strand | P52888 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 943 | 0.76 | 0.78 | 86 | empty |
| 2 | 1083 | 0.73 | 0.76 | 81 | empty |
| 3 | 79 | 0.45 | 0.81 | 15 | empty |
| 4 | 53 | 0.35 | 0.79 | 17 | empty |
| 5 | 56 | 0.31 | 0.76 | 11 | 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 P52888
- Elsewhere: RCSB PDB 1S4B · PDBe 1S4B · UniProt P52888
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