MolNFT v1 · #30550 · protein
X-ray structure of human N-acetyl galactosamine kinase complexed with mn-amppnp and N-acetyl glactosamine
2A2D · N-acetylgalactosamine kinase: “X-ray structure of human N-acetyl galactosamine kinase complexed with mn-amppnp and N-acetyl glactosamine”. X-ray diffraction, 3 ligands (ANP, A2G, MN), 3 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 2A2D
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylgalactosamine kinase
- EC
- 2.7.1.-
- UniProt
- Q01415
- Ligands
- ANP, A2G, MN
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylgalactosamine kinase (EC 2.7.1.-) | protein | 448 | 46% helix, 19% strand | Q01415 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.79 | 0.90 | 51 | A2G, MN, ANP |
| 2 | 177 | 0.52 | 0.78 | 26 | empty |
| 3 | 112 | 0.38 | 0.75 | 15 | empty |
Compared structures
- 2A2D · X-ray structure of human n-acetyl galactosamine kinase complexed with Mn-AMPPNP and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01415 · AlphaFold monomer V2.0 prediction for N-acetylgalactosamine kinase (Q01415) · a predicted model of the same protein · chain A 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 Q01415
- Elsewhere: RCSB PDB 2A2D · PDBe 2A2D · UniProt Q01415
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