Research workbench
Three dimensional structure of de novo designed serine hydrolase OSH26, northeast structural genomics consortium (nesg) target OR89
Analyse Three dimensional structure of de novo designed serine hydrolase OSH26… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DRT
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo designed serine hydrolase, OR89
- Ligands
- NA, CL
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | De novo designed serine hydrolase, OR89 | protein | 352 | 27% helix, 33% strand | — |
Ligands and binding sites
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 | 99 | 0.46 | 0.80 | 19 | empty |
| 2 | 105 | 0.38 | 0.74 | 20 | empty |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 4DRT · Three dimensional structure of de novo designed serine hydrolase OSH26, Northeast… · 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
- Elsewhere: RCSB PDB 4DRT · PDBe 4DRT
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