Research workbench
Crystal structure of red chlorophyll catabolite reductase from arabidopsis thaliana
Analyse Crystal structure of red chlorophyll catabolite reductase from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZXL
- Type
- protein
- Length
- 557 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Red chlorophyll catabolite reductase, chloroplastic
- EC
- 1.3.1.80
- UniProt
- Q8LDU4
- Ligands
- NA, SO4
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Red chlorophyll catabolite reductase, chloroplastic (EC 1.3.1.80) | protein | 279 | 47% helix, 22% strand | Q8LDU4 |
| B | Red chlorophyll catabolite reductase, chloroplastic (EC 1.3.1.80) | protein | 278 | 46% helix, 19% strand | Q8LDU4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.83 | 0.89 | 45 | empty |
| 2 | 448 | 0.75 | 0.83 | 42 | empty |
| 3 | 409 | 0.72 | 0.82 | 40 | empty |
| 4 | 132 | 0.46 | 0.78 | 20 | empty |
| 5 | 62 | 0.35 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1102 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2ZXL · Crystal structure of red chlorophyll catabolite reductase from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q8LDU4 · AlphaFold monomer V2.0 prediction for red chlorophyll catabolite reductase, chloroplastic… · 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 Q8LDU4
- Elsewhere: RCSB PDB 2ZXL · PDBe 2ZXL · UniProt Q8LDU4
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