Research workbench
Haloferax volcanii malate synthase PYRUVATE/ACETYL-CoA ternary complex
Analyse Haloferax volcanii malate synthase PYRUVATE/ACETYL-CoA ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OYZ
- Type
- protein
- Length
- 376 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
- ACO, PYR, K, MG, CL, PO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malate synthase (EC 2.3.3.9) | protein | 376 | 50% helix, 13% strand | D4GTL2 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
- PYR · Pyruvic acid · ligand · chains A
- K · Potassium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.65 | 0.84 | 32 | ACO, PYR, MG |
| 2 | 224 | 0.65 | 0.83 | 38 | empty |
| 3 | 164 | 0.53 | 0.79 | 28 | empty |
| 4 | 97 | 0.38 | 0.76 | 21 | empty |
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 3OYZ · PDBe 3OYZ · UniProt D4GTL2
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