MolNFT v2 · #82237 · protein
Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae
3VFL: “Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus…”. X-ray diffraction at 1.91. MolNFT v2 #82237 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3VFL
- Type
- protein
- Length
- 614 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.91
- Source
- Streptococcus pneumoniae
- UniProt
- A5LD17
Structure
x-ray diffraction · resolution 1.91 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | A5LD17 |
| B | — | protein | 306 | — | A5LD17 |
Compared structures
- 3VFL · Structure, function, stability and knockout phenotype of dihydrodipicolinate synthase… · 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
- Every structure of UniProt A5LD17
- Elsewhere: RCSB PDB 3VFL · PDBe 3VFL · UniProt A5LD17
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