MolNFT v1 · #107365 · protein
Human PIN1 with S-hydroxyl-cysteine 113
4U84 · Peptidyl-prolyl cis-trans isomerase nima-interacting 1: “Human PIN1 with S-hydroxyl-cysteine 113”. X-ray diffraction, 2 pockets (best druggability 0.30). MolNFT v1 #107365 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4U84
- Type
- protein
- Length
- 145 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase nima-interacting 1
- EC
- 5.2.1.8
- UniProt
- Q13526
- Pockets
- 2 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8) | protein | 145 | 27% helix, 28% strand | Q13526 |
Ligands and binding sites
- 15P · Polyethylene glycol (N=34) · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.30 | 0.76 | 15 | empty |
| 2 | 73 | 0.30 | 0.73 | 16 | 15P |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4U84 · Human Pin1 with S-hydroxyl-cysteine 113 · 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 4U84 · PDBe 4U84 · UniProt Q13526
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