MolNFT v1 · #37717 · protein
T152C mutant glycosylasparaginase from flavobacterium meningosepticum
2GAC: “T152C mutant glycosylasparaginase from flavobacterium meningosepticum”. X-ray diffraction, 6 pockets (best druggability 0.56). MolNFT v1 #37717 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GAC
- Type
- protein
- Length
- 550 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosylasparaginase
- EC
- 3.5.1.26
- UniProt
- Q47898
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glycosylasparaginase (EC 3.5.1.26) | protein | 136 | 46% helix, 15% strand | Q47898 |
| B, D | Glycosylasparaginase (EC 3.5.1.26) | protein | 139 | 27% helix, 35% strand | Q47898 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.56 | 0.86 | 26 | empty |
| 2 | 69 | 0.51 | 0.85 | 17 | empty |
| 3 | 62 | 0.47 | 0.84 | 16 | empty |
| 4 | 152 | 0.46 | 0.77 | 23 | empty |
| 5 | 140 | 0.45 | 0.77 | 25 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2642 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 2636 Ų buried · 49 hydrogen bonds · protein-protein
- A–D · 721 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 719 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 690 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2GAC · T152C mutant glycosylasparaginase from flavobacterium meningosepticum · the same entry in another collection · chain D against D, TM-score 1.00
- Q47898 · AlphaFold monomer V2.0 prediction for N(4)-(beta-N- acetylglucosaminyl)-L-asparaginase… · a predicted model of the same protein · chain C 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 Q47898
- Elsewhere: RCSB PDB 2GAC · PDBe 2GAC · UniProt Q47898
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