Research workbench
Crystal structure of a haloacid dehalogenase-like hydrolase (target efi-900331) from bacteroides thetaiotaomicron with bound mg crystal form II
Analyse Crystal structure of a haloacid dehalogenase-like hydrolase (target efi-900331)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DWO
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haloacid dehalogenase-like hydrolase
- EC
- 3.8.1.-
- UniProt
- Q8A2F3
- Ligands
- MG
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Haloacid dehalogenase-like hydrolase (EC 3.8.1.-) | protein | 268 | 43% helix, 23% strand | Q8A2F3 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.58 | 0.83 | 29 | GOL |
| 2 | 68 | 0.32 | 0.75 | 17 | empty |
Compared structures
- 4DWO · Crystal structure of a haloacid dehalogenase-like hydrolase (Target EFI-900331) from… · 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 Q8A2F3
- Elsewhere: RCSB PDB 4DWO · PDBe 4DWO · UniProt Q8A2F3
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