MolNFT v1 · #18240 · protein
PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens
1PIN: “PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens”. X-ray diffraction, 2 ligands (1PG, SO4), 1 pocket (best druggability 0.29). MolNFT v1 #18240 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PIN
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q13526
- Ligands
- 1PG, SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 155 | 25% helix, 23% strand | Q13526 |
Ligands and binding sites
- 1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.29 | 0.76 | 14 | empty |
Compared structures
- 1PIN · PIN1 peptidyl-prolyl cis-trans isomerase from homo sapiens · 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 Q13526
- Elsewhere: RCSB PDB 1PIN · PDBe 1PIN · UniProt Q13526
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