Research workbench
Crystal structure of type II MALATE/LACTATE dehydrogenase from thermus thermophilus HB8
Analyse Crystal structure of type II MALATE/LACTATE dehydrogenase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X0A
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALATE/L-lactate dehydrogenase family protein
- EC
- 1.1.1.27
- UniProt
- Q53W84
- Ligands
- NA
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MALATE/L-lactate dehydrogenase family protein (EC 1.1.1.27) | protein | 344 | 44% helix, 18% strand | Q53W84 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.67 | 0.82 | 67 | NA, FMT |
| 2 | 102 | 0.41 | 0.77 | 20 | empty |
| 3 | 57 | 0.35 | 0.78 | 10 | empty |
Compared structures
- 1X0A · Crystal Structure of type II malate/lactate dehydrogenase from thermus thermophilus HB8 · 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 Q53W84
- Elsewhere: RCSB PDB 1X0A · PDBe 1X0A · UniProt Q53W84
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