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Crystal structure of mutant 2-methylcitrate synthase (MCSAG352A) from aspergillus fumigatus
Analyse Crystal structure of mutant 2-methylcitrate synthase (MCSAG352A) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UQU
- Type
- protein
- Length
- 874 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q50I20
- Ligands
- OAA, COA, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 438 | — | Q50I20 |
| B | — | protein | 436 | — | Q50I20 |
Ligands and binding sites
- OAA · Oxaloacetate ion · ligand · chains A, B
- COA · Coenzyme A · ligand · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UQU · Crystal structure of mutant 2-methylcitrate synthase (mcsAG352A) from Aspergillus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q50I20 · AlphaFold monomer V2.0 prediction for 2-methylcitrate synthase, mitochondrial (Q50I20) · a predicted model of the same protein · 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 Q50I20
- Elsewhere: RCSB PDB 5UQU · PDBe 5UQU · UniProt Q50I20
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