Research workbench
Cyclophilin a complexed with succinyl-ala-pro-ala-P-nitroanilide
Analyse Cyclophilin a complexed with succinyl-ala-pro-ala-P-nitroanilide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LOP
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclophilin a; Succinyl-ala-pro-ala-P-nitroanilide
- EC
- 5.2.1.8
- UniProt
- P23869
- Ligands
- NIT
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclophilin a (EC 5.2.1.8) | protein | 164 | 14% helix, 35% strand | P23869 |
| B | Succinyl-ala-pro-ala-P-nitroanilide | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
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 | 80 | 0.32 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 220 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct, covalent ligand).
Compared structures
- 1LOP · Cyclophilin a complexed with succinyl-ala-pro-ala-P-nitroanilide · the same entry in another collection · chain A against A, TM-score 1.00
- P23869 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase B (P23869) · a predicted model of the same protein · 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 P23869
- Elsewhere: RCSB PDB 1LOP · PDBe 1LOP · UniProt P23869
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