MolNFT v1 · #64457 · protein
Crystal structure of GCN5-related N-acetyltransferase-like protein (ZP_00874857) (ZP_00874857.1) from streptococcus suis 89/1591 at 1.80 a resolution
3G3S: “Crystal structure of GCN5-related N-acetyltransferase-like protein (ZP_00874857) (ZP_00874857.1) from…”. X-ray diffraction, 1 ligand (NA), 8 pockets (best druggability 0.58). MolNFT v1 #64457 on GenesisL1: 3D structure, binding…
- PDB
- 3G3S
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GCN5-related N-acetyltransferase
- UniProt
- Q302C5
- Ligands
- NA
- Pockets
- 8 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GCN5-related N-acetyltransferase | protein | 249 | 39% helix, 31% strand | Q302C5 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A, B
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
- CAC · Cacodylate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.58 | 0.77 | 39 | EDO |
| 2 | 266 | 0.58 | 0.78 | 38 | CAC, EDO |
| 3 | 290 | 0.54 | 0.76 | 39 | EDO |
| 4 | 81 | 0.41 | 0.79 | 19 | EDO |
| 5 | 74 | 0.33 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 622 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3G3S · Crystal structure of GCN5-related N-acetyltransferase-like protein (ZP_00874857)… · the same entry in another collection · chain A 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 Q302C5
- Elsewhere: RCSB PDB 3G3S · PDBe 3G3S · UniProt Q302C5
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