MolNFT v1 · #168770 · protein
Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N- succinyltransferase from bartonella henselae
6WQM: “Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N- succinyltransferase from bartonella henselae”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #168770 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6WQM
- Type
- protein
- Length
- 1,681 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6G549
- Ligands
- CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | — | protein | 280 | — | Q6G549 |
| B | — | protein | 279 | — | Q6G549 |
| C | — | protein | 280 | — | Q6G549 |
| D, E | — | protein | 281 | — | Q6G549 |
Ligands and binding sites
- CL · Chloride ion · ion · 7 copies · chains A, C, B, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WQM · Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase from… · the same entry in another collection · chain F against F, TM-score 1.00
- Q6G549 · AlphaFold monomer V2.0 prediction for 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate… · a predicted model of the same protein · chain F against A, TM-score 0.99
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 Q6G549
- Elsewhere: RCSB PDB 6WQM · PDBe 6WQM · UniProt Q6G549
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