Research workbench
L-fuculose 1-phosphate aldolase from escherichia COLI mutant S71Q
Analyse L-fuculose 1-phosphate aldolase from escherichia COLI mutant S71Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E4C
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-fuculose 1-phosphate aldolase
- EC
- 4.1.2.17
- UniProt
- P11550
- Ligands
- ZN, SO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | L-fuculose 1-phosphate aldolase (EC 4.1.2.17) | protein | 206 | 44% helix, 16% strand | P11550 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains P
- SO4 · Sulfate ion · ion · chains P
- BME · Beta-mercaptoethanol · additive · chains P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 1E4C · L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant S71Q · 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 P11550
- Elsewhere: RCSB PDB 1E4C · PDBe 1E4C · UniProt P11550
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