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Crystal structure of the rrm domain of CYP33
Analyse Crystal structure of the rrm domain of CYP33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LPY
- Type
- protein
- Length
- 158 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase E
- EC
- 5.2.1.8
- UniProt
- Q9UNP9
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8) | protein | 79 | 28% helix, 33% strand | Q9UNP9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
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 | 76 | 0.31 | 0.73 | 14 | EPE |
| 2 | 68 | 0.29 | 0.73 | 16 | EPE |
Interfaces
1 interface between chains.
- A–B · 598 Ų buried · 9 hydrogen bonds · protein-protein
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 Q9UNP9
- Elsewhere: RCSB PDB 3LPY · PDBe 3LPY · UniProt Q9UNP9
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