Research workbench
Cystal structure of arabidopsis ATR2
Analyse Cystal structure of arabidopsis ATR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GXU
- Type
- protein
- Length
- 946 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH--cytochrome P450 reductase 2
- EC
- 1.6.2.4
- UniProt
- Q9SUM3
- Ligands
- FAD, FMN
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH--cytochrome P450 reductase 2 (EC 1.6.2.4) | protein | 552 | 40% helix, 21% strand | Q9SUM3 |
| B | NADPH--cytochrome P450 reductase 2 (EC 1.6.2.4) | protein | 394 | 36% helix, 21% strand | Q9SUM3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- FMN · Flavin mononucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1195 | 0.80 | 0.81 | 128 | FAD |
| 2 | 840 | 0.74 | 0.78 | 62 | empty |
| 3 | 493 | 0.63 | 0.76 | 57 | FAD |
| 4 | 190 | 0.60 | 0.82 | 29 | FMN |
| 5 | 97 | 0.41 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 590 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q9SUM3
- Elsewhere: RCSB PDB 5GXU · PDBe 5GXU · UniProt Q9SUM3
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