MolNFT v1 · #36765 · protein
Crystal structure of human ppgalnact-2 complexed with udp and EA2
2FFU · Polypeptide N-acetylgalactosaminyltransferase 2: “Crystal structure of human ppgalnact-2 complexed with udp and EA2”. X-ray diffraction, 2 ligands (UDP, MN), 3 pockets (best druggability 0.79). MolNFT v1 #36765 on GenesisL1: 3D…
- PDB
- 2FFU
- Type
- protein
- Length
- 503 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polypeptide N-acetylgalactosaminyltransferase 2; 13-peptide EA2, pttdsttpapttk
- EC
- 2.4.1.41
- UniProt
- Q10471
- Ligands
- UDP, MN
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) | protein | 494 | 30% helix, 24% strand | Q10471 |
| P | 13-peptide EA2, pttdsttpapttk | protein | 9 | 0% helix, 11% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.79 | 0.92 | 50 | UDP |
| 2 | 76 | 0.45 | 0.81 | 17 | empty |
| 3 | 50 | 0.29 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–P · 600 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 2FFU · Crystal Structure of Human ppGalNAcT-2 complexed with UDP and EA2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q10471 · AlphaFold monomer V2.0 prediction for polypeptide N-acetylgalactosaminyltransferase 2… · a predicted model of the same protein · chain A against A, TM-score 0.81
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 Q10471
- Elsewhere: RCSB PDB 2FFU · PDBe 2FFU · UniProt Q10471
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.