Research workbench
Crystal structure of N-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and L-arginine
Analyse Crystal structure of N-acetylglutamate synthase from neisseria gonorrhoeae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D2P
- Type
- protein
- Length
- 848 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acetylglutamate synthase
- EC
- 2.3.1.1
- UniProt
- Q5FAK7
- Ligands
- COA, ARG
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative acetylglutamate synthase (EC 2.3.1.1) | protein | 424 | 38% helix, 26% strand | Q5FAK7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.82 | 0.98 | 38 | empty |
| 2 | 465 | 0.65 | 0.78 | 47 | COA |
| 3 | 413 | 0.65 | 0.78 | 44 | COA |
| 4 | 161 | 0.62 | 0.85 | 32 | empty |
| 5 | 180 | 0.58 | 0.81 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 1292 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3D2P · Crystal structure of N-acetylglutamate synthase from Neisseria gonorrhoeae complexed with… · 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 Q5FAK7
- Elsewhere: RCSB PDB 3D2P · PDBe 3D2P · UniProt Q5FAK7
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