Research workbench
Crystal structure of a terephthalate 1,2-cis- dihydrodioldehydrogenase from burkholderia xenovorans LB400
Analyse Crystal structure of a terephthalate 1,2-cis- dihydrodioldehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ATY
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Terephthalate 1,2-cis-dihydrodiol dehydrogenase
- EC
- 1.1.1.262
- UniProt
- Q13RP4
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Terephthalate 1,2-cis-dihydrodiol dehydrogenase (EC 1.1.1.262) | protein | 309 | 43% helix, 17% strand | Q13RP4 |
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 | 202 | 0.48 | 0.75 | 35 | empty |
| 2 | 62 | 0.31 | 0.75 | 15 | empty |
Compared structures
- 4ATY · Crystal structure of a Terephthalate 1,2-cis-dihydrodioldehydrogenase from Burkholderia… · 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 Q13RP4
- Elsewhere: RCSB PDB 4ATY · PDBe 4ATY · UniProt Q13RP4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.