MolNFT v1 · #146322 · protein
Crystal structure of the double mutant (D52N/L375F) of the full-length NT5C2 in the active state
6DE2: “Crystal structure of the double mutant (D52N/L375F) of the full-length NT5C2 in the active state”. X-ray diffraction, 3 ligands (ATP, MG, PO4). MolNFT v1 #146322 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DE2
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49902
- Ligands
- ATP, MG, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 472 | — | P49902 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DE2 · Crystal structure of the double mutant (D52N/L375F) of the full-length NT5C2 in the… · the same entry in another collection · chain A against A, TM-score 1.00
- P49902 · AlphaFold monomer V2.0 prediction for cytosolic purine 5'-nucleotidase (P49902) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P49902
- Elsewhere: RCSB PDB 6DE2 · PDBe 6DE2 · UniProt P49902
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