MolNFT v2 · #57669 · protein
Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark
3AEQ: “Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in…”. X-ray diffraction at 2.9. MolNFT v2 #57669 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3AEQ
- Type
- protein
- Length
- 1,667 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Rhodobacter capsulatus
- UniProt
- P26164, P26163
Structure
x-ray diffraction · resolution 2.9 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 415 | — | P26164 |
| B, D | — | protein | 419 | — | P26163 |
| C | — | protein | 414 | — | P26164 |
Compared structures
- 3AEQ · Structure of the light-independent protochlorophyllide reductase catalyzing a key… · the same entry in another collection · chain D against D, TM-score 1.00
- 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
- 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
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 3AEQ · PDBe 3AEQ · UniProt P26164 · UniProt P26163
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