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Structure of actinorhodin polyketide (actiii) reductase
Analyse Structure of actinorhodin polyketide (actiii) reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W4Z
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketoacyl reductase
- EC
- 1.3.1.-
- UniProt
- P16544
- Ligands
- NAP
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ketoacyl reductase (EC 1.3.1.-) | protein | 259 | 51% helix, 15% strand | P16544 |
| B | Ketoacyl reductase (EC 1.3.1.-) | protein | 261 | 50% helix, 15% strand | P16544 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- FMT · Formic acid · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 691 | 0.75 | 0.80 | 56 | NAP, FMT |
| 2 | 525 | 0.74 | 0.82 | 58 | NAP |
Interfaces
1 interface between chains.
- A–B · 1657 Ų buried · 17 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 P16544
- Elsewhere: RCSB PDB 1W4Z · PDBe 1W4Z · UniProt P16544
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