MolNFT v2 · #63454 · protein
Crystal structure of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member, trigonal crystal form
3FA3: “Crystal structure of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member, trigonal…”. X-ray diffraction at 2.6. MolNFT v2 #63454 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FA3
- Type
- protein
- Length
- 4,795 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Aspergillus niger
- UniProt
- Q2L887
Structure
x-ray diffraction · resolution 2.6 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F, G, H, O, P | — | protein | 301 | — | Q2L887 |
| B | — | protein | 302 | — | Q2L887 |
| I, K, M | — | protein | 300 | — | Q2L887 |
| J, N | — | protein | 292 | — | Q2L887 |
| L | — | protein | 300 | — | Q2L887 |
Compared structures
- 3FA3 · Crystal structure of 2,3-dimethylmalate lyase, a pep MUTASE/ISOCITRATE lyase superfamily… · 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 Q2L887
- Elsewhere: RCSB PDB 3FA3 · PDBe 3FA3 · UniProt Q2L887
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