Research workbench
Two-state solution NMR structure of PIN1 bound to peptide ffpspr
Analyse Two-state solution NMR structure of PIN1 bound to peptide ffpspr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SUQ
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- solution nmr
- 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
- 1 · best druggability 0.47
Structure
solution nmr · 1 distinct chain · 17% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8) | protein | 163 | 17% helix, 4% strand | Q13526 |
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 | 145 | 0.47 | 0.77 | 27 | empty |
Compared structures
- 7SUQ · Two-state solution NMR structure of Pin1 bound to peptide FFpSPR · 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 7SUQ · PDBe 7SUQ · UniProt Q13526
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