Research workbench
Structure of a short-chain type DEHYDROGENASE/REDUCTASE from mycobacterium ulcerans
Analyse Structure of a short-chain type DEHYDROGENASE/REDUCTASE from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TL3
- Type
- protein
- Length
- 470 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short-chain type DEHYDROGENASE/REDUCTASE
- EC
- 1.-.-.-
- UniProt
- A0PMN1
- Ligands
- NA
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Short-chain type DEHYDROGENASE/REDUCTASE (EC 1.-.-.-) | protein | 236 | 51% helix, 18% strand | A0PMN1 |
| B | Short-chain type DEHYDROGENASE/REDUCTASE (EC 1.-.-.-) | protein | 234 | 46% helix, 18% strand | A0PMN1 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.73 | 0.86 | 45 | empty |
| 2 | 251 | 0.61 | 0.80 | 30 | empty |
| 3 | 229 | 0.48 | 0.74 | 31 | empty |
| 4 | 166 | 0.46 | 0.75 | 27 | empty |
| 5 | 111 | 0.44 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1013 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3TL3 · Structure of a short-chain type dehydrogenase/reductase from Mycobacterium ulcerans · 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 A0PMN1
- Elsewhere: RCSB PDB 3TL3 · PDBe 3TL3 · UniProt A0PMN1
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