Research workbench
Crystal structure of hypothetical protein with ketosteroid isomerase- like protein fold from catenulispora acidiphila dsm 44928
Analyse Crystal structure of hypothetical protein with ketosteroid isomerase- like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H3U
- Type
- protein
- Length
- 261 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- C7PVH9
- Ligands
- CD, CL
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 131 | 29% helix, 46% strand | C7PVH9 |
| B | Hypothetical protein | protein | 130 | 29% helix, 46% strand | C7PVH9 |
Ligands and binding sites
- CD · Cadmium ion · metal · 7 copies · chains A, B
- CL · Chloride ion · ion · 7 copies · chains A, B
- ACT · Acetate ion · additive · 4 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.58 | 0.83 | 38 | CL |
| 2 | 101 | 0.56 | 0.84 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 926 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4H3U · Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold… · 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 C7PVH9
- Elsewhere: RCSB PDB 4H3U · PDBe 4H3U · UniProt C7PVH9
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