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The crystal structure of methylglyoxal synthase from thermus sp. GH5 bound to malonate.
Analyse The crystal structure of methylglyoxal synthase from thermus sp. GH5 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X8W
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylglyoxal synthase
- EC
- 4.2.99.11
- UniProt
- B3VH91
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylglyoxal synthase (EC 4.2.99.11) | protein | 125 | 54% helix, 16% strand | B3VH91 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2X8W · The Crystal Structure of Methylglyoxal Synthase from Thermus sp. GH5 Bound to Malonate. · 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 B3VH91
- Elsewhere: RCSB PDB 2X8W · PDBe 2X8W · UniProt B3VH91
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