Research workbench
Crystal structure of a domain swapped 2,3,4,5-tetrahydropyridine-2,6- dicarboxylate N-succinyltransferase from acinetobacter baumannii
Analyse Crystal structure of a domain swapped 2,3,4,5-tetrahydropyridine-2,6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AMZ
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N- succinyltransferase
- EC
- 2.3.1.117
- UniProt
- Q5DL43
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N- succinyltransferase (EC 2.3.1.117) | protein | 256 | 20% helix, 28% strand | Q5DL43 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6AMZ · Crystal structure of a domain swapped 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5DL43 · AlphaFold monomer V2.0 prediction for 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate… · a predicted model of the same protein · chain A against A, TM-score 0.70
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 Q5DL43
- Elsewhere: RCSB PDB 6AMZ · PDBe 6AMZ · UniProt Q5DL43
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.