Research workbench
Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark
Analyse Structure of the light-independent protochlorophyllide reductase catalyzing a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AEK
- Type
- protein
- Length
- 1,665 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P26164, P26163
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 415 | — | P26164 |
| B, D | — | protein | 418 | — | P26163 |
| C | — | protein | 414 | — | P26164 |
Compared structures
- 3AEK · Structure of the light-independent protochlorophyllide reductase catalyzing a key… · the same entry in another collection · chain D against D, TM-score 1.00
- P26163 · AlphaFold monomer V2.0 prediction for light-independent protochlorophyllide reductase… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P26164 · AlphaFold monomer V2.0 prediction for light-independent protochlorophyllide reductase… · a predicted model of the same protein · chain A 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 P26164
- Every structure of UniProt P26163
- Elsewhere: RCSB PDB 3AEK · PDBe 3AEK · UniProt P26164 · UniProt P26163
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