Research workbench
Three-dimensional structure of E. COLI dihydrodipicolinate reductase
Analyse Three-dimensional structure of E. COLI dihydrodipicolinate reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DIH
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrodipicolinate reductase
- EC
- 1.3.1.26
- UniProt
- P04036
- Ligands
- NDP
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrodipicolinate reductase (EC 1.3.1.26) | protein | 272 | 33% helix, 22% strand | P04036 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.54 | 0.75 | 45 | NDP |
| 2 | 130 | 0.42 | 0.75 | 18 | empty |
Compared structures
- 1DIH · Three-dimensional structure of E. COLI dihydrodipicolinate reductase · the same entry in another collection · chain A against A, TM-score 1.00
- P04036 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (P04036) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P04036
- Elsewhere: RCSB PDB 1DIH · PDBe 1DIH · UniProt P04036
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