Research workbench
Haloferax volcanii malate synthase LEAD(II) complex
Analyse Haloferax volcanii malate synthase LEAD(II) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TAO
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malate synthase
- EC
- 2.3.3.9
- UniProt
- D4GTL2
- Ligands
- GLV, PB, K, NA, CL
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malate synthase (EC 2.3.3.9) | protein | 356 | 53% helix, 11% strand | D4GTL2 |
Ligands and binding sites
- GLV · Glyoxylic acid · ligand · 3 copies · chains A
- PB · Lead (II) ion · metal · 4 copies · chains A
- K · Potassium ion · metal · 3 copies · chains A
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- ACT · Acetate ion · additive · chains A
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 | 619 | 0.67 | 0.77 | 70 | GLV |
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 D4GTL2
- Elsewhere: RCSB PDB 5TAO · PDBe 5TAO · UniProt D4GTL2
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