MolNFT v1 · #160184 · protein
Pntc-aept: fusion protein of phosphonate-specific cytidylyltransferase and 2-aminoethylphosphonate (aep) transaminase from treponema denticola in complex with cytidine monophosphate-aep
6PD2: “Pntc-aept: fusion protein of phosphonate-specific cytidylyltransferase and 2-aminoethylphosphonate (aep)…”. X-ray diffraction, 4 ligands (PLP, 0RC, MG). MolNFT v1 #160184 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PD2
- Type
- protein
- Length
- 2,454 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q73MU2
- Ligands
- PLP, 0RC, MG, PO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 615 | — | Q73MU2 |
| C | — | protein | 616 | — | Q73MU2 |
| D | — | protein | 608 | — | Q73MU2 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, C, B, D
- 0RC · 5'-O-[(S)-{[(R)-(2-aminoethyl)(hydroxy) phosphoryl]oxy}(hydroxy)phosphoryl]cytidine · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 11 copies · chains A, C, B, D
- EDO · 1,2-ethanediol · additive · 27 copies · chains A, B, D, C
- ACT · Acetate ion · additive · 3 copies · chains A, C
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PD2 · PntC-AEPT: fusion protein of phosphonate-specific cytidylyltransferase and… · 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 Q73MU2
- Elsewhere: RCSB PDB 6PD2 · PDBe 6PD2 · UniProt Q73MU2
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