MolNFT v1 · #90509 · protein
Structure-activity relationship guides enantiomeric preference among potent inhibitors of B. anthracis dihydrofolate reductase
4ELG: “Structure-activity relationship guides enantiomeric preference among potent inhibitors of B. anthracis…”. X-ray diffraction. MolNFT v1 #90509 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4ELG
- Type
- protein
- Length
- 1,328 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q81R22
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | — | protein | 166 | — | Q81R22 |
Compared structures
- 4ELG · Structure-activity relationship guides enantiomeric preference among potent inhibitors of… · 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 Q81R22
- Elsewhere: RCSB PDB 4ELG · PDBe 4ELG · UniProt Q81R22
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