Research workbench
Schiff-base complex of yeast 5-aminolaevulinic acid dehydratase with 5-aminolaevulinic acid at 1.7 a resolution
Analyse Schiff-base complex of yeast 5-aminolaevulinic acid dehydratase with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H7O
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- SACCHAROMYCES CEREVISIAE
- Molecule
- 5-aminolaevulinic acid dehydratase
- EC
- 4.2.1.24
- UniProt
- P05373
- Ligands
- DAV, ZN
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-aminolaevulinic acid dehydratase (EC 4.2.1.24) | protein | 341 | 41% helix, 16% strand | P05373 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.36 | 0.75 | 24 | empty |
| 2 | 66 | 0.36 | 0.76 | 13 | empty |
| 3 | 100 | 0.35 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1H7O · Schiff-base complex of yeast 5-aminolaevulinic acid dehydratase with 5-aminolaevulinic… · the same entry in another collection · chain A against A, TM-score 1.00
- P05373 · AlphaFold monomer V2.0 prediction for delta-aminolevulinic acid dehydratase (P05373) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P05373
- Elsewhere: RCSB PDB 1H7O · PDBe 1H7O · UniProt P05373
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