Research workbench
Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with NADH, oxalate and metal ion
Analyse Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FLK
- Type
- protein
- Length
- 1,436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tartrate DEHYDROGENASE/DECARBOXYLASE
- EC
- 1.1.1.93
- UniProt
- Q51945
- Ligands
- NAI, OXL, MG, SO4, NH4
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tartrate DEHYDROGENASE/DECARBOXYLASE (EC 1.1.1.93) | protein | 359 | 42% helix, 21% strand | Q51945 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- OXL · Oxalate ion · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 14 copies · chains A, B, C, D
- NH4 · Ammonium ion · ion · 4 copies · chains A, B, C, D
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 3 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.75 | 0.82 | 60 | MG, NAI, OXL |
| 2 | 625 | 0.75 | 0.82 | 60 | MG, NAI, OXL |
| 3 | 541 | 0.75 | 0.83 | 57 | MG, DTT, NAI, OXL |
| 4 | 613 | 0.75 | 0.81 | 62 | MG, NAI, OXL, NH4 |
| 5 | 462 | 0.68 | 0.79 | 55 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2716 Ų buried · 55 hydrogen bonds · protein-protein
- C–D · 2714 Ų buried · 58 hydrogen bonds · protein-protein
- A–C · 661 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 653 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 171 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 modified (engineered).
Compared structures
- 3FLK · Crystal Structure of Tartrate Dehydrogenase from Pseudomonas putida in complex with NADH… · the same entry in another collection · chain B against B, TM-score 1.00
- Q51945 · AlphaFold monomer V2.0 prediction for tartrate DEHYDROGENASE/DECARBOXYLASE (Q51945) · a predicted model of the same protein · 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 Q51945
- Elsewhere: RCSB PDB 3FLK · PDBe 3FLK · UniProt Q51945
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