MolNFT v1 · #143803 · protein
Crystal structure of aspartate-semialdehyde dehydrogenase from neisseria gonorrhoeae
6BAC: “Crystal structure of aspartate-semialdehyde dehydrogenase from neisseria gonorrhoeae”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.58). MolNFT v1 #143803 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6BAC
- Type
- protein
- Length
- 373 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate-semialdehyde dehydrogenase
- EC
- 1.2.1.11
- UniProt
- A0A1D3HC29
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) | protein | 373 | 40% helix, 23% strand | A0A1D3HC29 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.58 | 0.78 | 40 | EDO |
Compared structures
- 6BAC · Crystal Structure of Aspartate-Semialdehyde Dehydrogenase from Neisseria gonorrhoeae · 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 A0A1D3HC29
- Elsewhere: RCSB PDB 6BAC · PDBe 6BAC · UniProt A0A1D3HC29
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