MolNFT v1 · #26776 · protein
Structural basis for alteration of cofactor specificity of malate dehydrogenase from thermus flavus
1WZE: “Structural basis for alteration of cofactor specificity of malate dehydrogenase from thermus flavus”. X-ray diffraction, 1 ligand (NAD), 7 pockets (best druggability 0.61). MolNFT v1 #26776 on GenesisL1: 3D structure, binding sites…
- PDB
- 1WZE
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malate dehydrogenase
- EC
- 1.1.1.37
- UniProt
- P10584
- Ligands
- NAD
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Malate dehydrogenase (EC 1.1.1.37) | protein | 327 | 45% helix, 19% strand | P10584 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 471 | 0.61 | 0.75 | 62 | NAD |
| 2 | 348 | 0.58 | 0.76 | 45 | NAD |
| 3 | 197 | 0.52 | 0.78 | 34 | empty |
| 4 | 234 | 0.52 | 0.76 | 40 | empty |
| 5 | 103 | 0.44 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1662 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 1WZE · Structural basis for alteration of cofactor specificity of Malate dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P10584 · AlphaFold monomer V2.0 prediction for malate dehydrogenase (P10584) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P10584
- Elsewhere: RCSB PDB 1WZE · PDBe 1WZE · UniProt P10584
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