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Dipicolinate bound Dihydrodipicolinate reductase from Paenisporosarcina sp. TG-14
Analyse Dipicolinate bound Dihydrodipicolinate reductase from Paenisporosarcina sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z2E
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Paenisporosarcina sp. TG-14
- Molecule
- Dihydrodipicolinate reductase
- Ligands
- PDC
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrodipicolinate reductase | protein | 265 | 33% helix, 24% strand | — |
Ligands and binding sites
- PDC · Pyridine-2,6-dicarboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.54 | 0.76 | 41 | PDC |
Compared structures
- 5Z2E · Dipicolinate bound dihydrodipicolinate reductase from paenisporosarcina sp. tg-14 · 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
- Elsewhere: RCSB PDB 5Z2E · PDBe 5Z2E
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