Research workbench
Structure of malonyl-coenzyme a reductase from crenarchaeota in complex with NADP
Analyse Structure of malonyl-coenzyme a reductase from crenarchaeota in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DPL
- Type
- protein
- Length
- 1,415 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96YK1
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 354 | — | Q96YK1 |
| C | — | protein | 353 | — | Q96YK1 |
Compared structures
- 4DPL · Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with NadP · the same entry in another collection · chain A against A, TM-score 1.00
- Q96YK1 · AlphaFold monomer V2.0 prediction for malonyl-CoA reductase (Q96YK1) · 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 Q96YK1
- Elsewhere: RCSB PDB 4DPL · PDBe 4DPL · UniProt Q96YK1
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