MolNFT v2 · #159836 · protein
Crystal Structure Analysis of PIN1
6O33 · Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1: “Crystal Structure Analysis of PIN1”. X-ray diffraction at 1.74, 1 ligand (SO4), 1 pocket (best druggability 0.29). MolNFT v2 #159836 on GenesisL1: 3D structure, binding sites…
- PDB
- 6O33
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.74
- Source
- Homo sapiens
- Molecule
- Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; peptide
- EC
- 5.2.1.8
- UniProt
- Q13526
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · resolution 1.74 · 2 distinct chains · 25% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) | protein | 150 | 26% helix, 25% strand | Q13526 |
| B | peptide | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- 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 | 61 | 0.29 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 458 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
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 Q13526
- Elsewhere: RCSB PDB 6O33 · PDBe 6O33 · UniProt Q13526
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