MolNFT v1 · #29569 · protein
Human PIN1 ng mutant
1ZCN · Peptidyl-prolyl cis-trans isomerase nima-interacting 1: “Human PIN1 ng mutant”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.34). MolNFT v1 #29569 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZCN
- Type
- protein
- Length
- 143 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
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.34
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 | 143 | 27% helix, 28% strand | Q13526 |
Ligands and binding sites
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 | 69 | 0.34 | 0.76 | 18 | PO4, 1PE |
| 2 | 73 | 0.32 | 0.75 | 17 | empty |
Compared structures
- 1ZCN · human Pin1 Ng mutant · 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 1ZCN · PDBe 1ZCN · UniProt Q13526
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