Research workbench
L-fuculose-1-phosphate aldolase from escherichia COLI mutant R212A
Analyse L-fuculose-1-phosphate aldolase from escherichia COLI mutant R212A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DZX
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A037YR34
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | — | protein | 208 | — | A0A037YR34 |
Compared structures
- 1DZX · L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant R212A · the same entry in another collection · chain P against P, 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 A0A037YR34
- Elsewhere: RCSB PDB 1DZX · PDBe 1DZX · UniProt A0A037YR34
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