MolNFT v1 · #17439 · protein
Crystal structure of apo (iron-free) taud
1OTJ · Alpha-ketoglutarate-dependent taurine dioxygenase: “Crystal structure of apo (iron-free) taud”. X-ray diffraction, 2 ligands (TAU, CL), 12 pockets (best druggability 0.74). MolNFT v1 #17439 on GenesisL1: 3D structure, binding sites…
- PDB
- 1OTJ
- Type
- protein
- Length
- 1,120 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-ketoglutarate-dependent taurine dioxygenase
- EC
- 1.14.11.17
- UniProt
- P37610
- Ligands
- TAU, CL
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent taurine dioxygenase (EC 1.14.11.17) | protein | 281 | 26% helix, 30% strand | P37610 |
| B | Alpha-ketoglutarate-dependent taurine dioxygenase (EC 1.14.11.17) | protein | 279 | 26% helix, 29% strand | P37610 |
| C, D | Alpha-ketoglutarate-dependent taurine dioxygenase (EC 1.14.11.17) | protein | 280 | 27% helix, 27% strand | P37610 |
Ligands and binding sites
- TAU · 2-aminoethanesulfonic acid · ligand · 3 copies · chains A, B, C
- CL · Chloride ion · ion · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.74 | 0.87 | 43 | CL |
| 2 | 357 | 0.71 | 0.83 | 45 | empty |
| 3 | 326 | 0.70 | 0.83 | 47 | empty |
| 4 | 212 | 0.68 | 0.85 | 40 | CL, TAU |
| 5 | 142 | 0.68 | 0.89 | 39 | TAU |
Interfaces
6 interfaces between chains.
- A–B · 952 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 942 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 550 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 541 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 252 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P37610
- Elsewhere: RCSB PDB 1OTJ · PDBe 1OTJ · UniProt P37610
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