Research workbench
Complex of the catalytic portion of human hmg-CoA reductase with hmg, CoA, and NADP+
Analyse Complex of the catalytic portion of human hmg-CoA reductase with hmg, CoA, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DQA
- Type
- protein
- Length
- 1,614 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04035
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 409 | — | P04035 |
| B | — | protein | 405 | — | P04035 |
| C | — | protein | 404 | — | P04035 |
| D | — | protein | 396 | — | P04035 |
Compared structures
- 1DQA · Complex of the catalytic portion of human hmg-CoA reductase with hmg, CoA, and NADP+ · the same entry in another collection · chain D against D, TM-score 1.00
- P04035 · AlphaFold monomer V2.0 prediction for 3-hydroxy-3-methylglutaryl- coenzyme a reductase… · a predicted model of the same protein · chain D against A, TM-score 0.99
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 P04035
- Elsewhere: RCSB PDB 1DQA · PDBe 1DQA · UniProt P04035
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