Research workbench
Structure of kdpg aldolase E45N mutant
Analyse Structure of kdpg aldolase E45N mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WAU
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KHG/KDPG aldolase
- EC
- 4.1.2.14, 4.1.3.16
- UniProt
- P10177
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KHG/KDPG aldolase (EC 4.1.2.14, 4.1.3.16) | protein | 213 | 42% helix, 17% strand | P10177 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1WAU · Structure of KDPG Aldolase E45N mutant · 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 P10177
- Elsewhere: RCSB PDB 1WAU · PDBe 1WAU · UniProt P10177
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