Research workbench
Crystal structure of ketosteroid isomerase containing Y32F, D40N, Y57F and Y119F mutations in the equilenin-bound form
Analyse Crystal structure of ketosteroid isomerase containing Y32F, D40N, Y57F and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AI1
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketosteroid isomerase
- UniProt
- P07445
- Ligands
- EQU
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ketosteroid isomerase | protein | 120 | 32% helix, 38% strand | P07445 |
Ligands and binding sites
- EQU · Equilenin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.64 | 0.84 | 19 | EQU |
Compared structures
- 5AI1 · Crystal structure of ketosteroid isomerase containing Y32F, D40N, Y57F and Y119F… · 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 P07445
- Elsewhere: RCSB PDB 5AI1 · PDBe 5AI1 · UniProt P07445
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