MolNFT v1 · #141287 · protein
NADPH/PDA bound dihydrodipicolinate reductase from paenisporosarcina sp. tg-14
5Z2F: “NADPH/PDA bound dihydrodipicolinate reductase from paenisporosarcina sp. tg-14”. X-ray diffraction, 2 ligands (NAP, PDC), 2 pockets (best druggability 0.75). MolNFT v1 #141287 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5Z2F
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrodipicolinate reductase
- Ligands
- NAP, PDC
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrodipicolinate reductase | protein | 265 | 35% helix, 26% strand | — |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- 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
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.75 | 0.85 | 38 | NAP, PDC |
| 2 | 61 | 0.56 | 0.89 | 15 | empty |
Compared structures
- 5Z2F · NADPH/PDA 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 5Z2F · PDBe 5Z2F
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