Research workbench
Crystal structure of an ASPARTATE/GLUTAMATE racemase from escherichia COLI O157
Analyse Crystal structure of an ASPARTATE/GLUTAMATE racemase from escherichia COLI O157 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HQT
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ASPARTATE/GLUTAMATE racemase
- UniProt
- A0A0F6FBL7
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ASPARTATE/GLUTAMATE racemase | protein | 235 | 60% helix, 12% strand | A0A0F6FBL7 |
Ligands and binding sites
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5HQT · Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157 · 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 A0A0F6FBL7
- Elsewhere: RCSB PDB 5HQT · PDBe 5HQT · UniProt A0A0F6FBL7
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