Research workbench
Crystal structure of ketosteroid isomerase fold protein HMUK_0747
Analyse Crystal structure of ketosteroid isomerase fold protein HMUK_0747 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MJD
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketosteroid isomerase fold protein HMUK_0747
- UniProt
- C7NZX0
- Ligands
- MG, NA
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ketosteroid isomerase fold protein HMUK_0747 | protein | 113 | 31% helix, 45% strand | C7NZX0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.66 | 0.86 | 24 | empty |
| 2 | 170 | 0.62 | 0.84 | 22 | empty |
| 3 | 57 | 0.34 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1035 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4MJD · Crystal structure of ketosteroid isomerase fold protein Hmuk_0747 · 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 C7NZX0
- Elsewhere: RCSB PDB 4MJD · PDBe 4MJD · UniProt C7NZX0
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