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Crystal structure of yeast GNA1
Analyse Crystal structure of yeast GNA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I21
- Type
- protein
- Length
- 921 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine-phosphate N-acetyltransferase
- EC
- 2.3.1.4
- UniProt
- P43577
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 6 distinct chains · 36% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 155 | 36% helix, 35% strand | P43577 |
| B | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 157 | 38% helix, 34% strand | P43577 |
| M | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 156 | 35% helix, 33% strand | P43577 |
| N | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 147 | 37% helix, 35% strand | P43577 |
| X | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 150 | 34% helix, 31% strand | P43577 |
| Y | Glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) | protein | 156 | 35% helix, 32% strand | P43577 |
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1153 | 0.81 | 0.82 | 89 | empty |
| 2 | 685 | 0.76 | 0.81 | 61 | empty |
| 3 | 358 | 0.63 | 0.78 | 39 | empty |
| 4 | 342 | 0.61 | 0.78 | 40 | empty |
| 5 | 338 | 0.60 | 0.77 | 49 | empty |
Interfaces
8 interfaces between chains.
- X–Y · 2868 Ų buried · 49 hydrogen bonds · protein-protein
- A–B · 2828 Ų buried · 49 hydrogen bonds · protein-protein
- M–N · 2808 Ų buried · 47 hydrogen bonds · protein-protein
- B–Y · 482 Ų buried · 8 hydrogen bonds · protein-protein
- B–M · 252 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 27 modified (engineered).
Compared structures
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 P43577
- Elsewhere: RCSB PDB 1I21 · PDBe 1I21 · UniProt P43577
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