Research workbench
Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers
Analyse Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IV0
- Type
- protein
- Length
- 824 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O29610
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 412 | — | O29610 |
Compared structures
- 2IV0 · Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by… · the same entry in another collection · chain A against A, TM-score 1.00
- O29610 · AlphaFold monomer V2.0 prediction for isocitrate dehydrogenase [NADP] (O29610) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O29610
- Elsewhere: RCSB PDB 2IV0 · PDBe 2IV0 · UniProt O29610
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