Research workbench
Human PPGALNACT2 I253A/L310A mutant with EA2 and udp
Analyse Human PPGALNACT2 I253A/L310A mutant with EA2 and udp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E7I
- Type
- protein
- Length
- 503 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polypeptide N-acetylgalactosaminyltransferase 2; EA2
- EC
- 2.4.1.41
- UniProt
- Q10471, Q62605
- Ligands
- UDP, MN
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) | protein | 494 | 30% helix, 25% strand | Q10471 |
| P | EA2 | protein | 9 | 0% helix, 11% strand | Q62605 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.84 | 0.96 | 59 | UDP, MN |
| 2 | 114 | 0.42 | 0.77 | 21 | empty |
| 3 | 60 | 0.35 | 0.77 | 15 | empty |
| 4 | 51 | 0.27 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–P · 646 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6E7I · Human ppGalNAcT2 I253A/L310A Mutant with EA2 and UDP · 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 0.80
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
- Every structure of UniProt Q62605
- Elsewhere: RCSB PDB 6E7I · PDBe 6E7I · UniProt Q10471 · UniProt Q62605
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