Research workbench
The structure of rice defective pollen wall (dpw) in the complex with its cofactor NADP
Analyse The structure of rice defective pollen wall (dpw) in the complex with its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EOZ
- Type
- protein
- Length
- 955 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acyl-CoA reductase
- EC
- 1.2.1.84
- UniProt
- Q0DUU1
- Ligands
- NAP
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acyl-CoA reductase (EC 1.2.1.84) | protein | 482 | 44% helix, 10% strand | Q0DUU1 |
| B | Fatty acyl-CoA reductase (EC 1.2.1.84) | protein | 473 | 44% helix, 10% strand | Q0DUU1 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.82 | 0.87 | 66 | NAP |
| 2 | 585 | 0.82 | 0.87 | 63 | NAP |
| 3 | 536 | 0.81 | 0.87 | 47 | empty |
| 4 | 737 | 0.72 | 0.79 | 101 | empty |
| 5 | 102 | 0.55 | 0.84 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 970 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7EOZ · The structure of rice Defective Pollen Wall (DPW) in the complex with its cofactor NADP · the same entry in another collection · 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 Q0DUU1
- Elsewhere: RCSB PDB 7EOZ · PDBe 7EOZ · UniProt Q0DUU1
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