Research workbench
Crystal structure of (R)-carbonyl reductase from candida parapsilosis in complex with NAD
Analyse Crystal structure of (R)-carbonyl reductase from candida parapsilosis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WLE
- Type
- protein
- Length
- 1,340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- (R)-specific carbonyl reductase
- EC
- 1.1.1.1
- UniProt
- A1X808
- Ligands
- NAD, ZN
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | (R)-specific carbonyl reductase (EC 1.1.1.1) | protein | 335 | 29% helix, 30% strand | A1X808 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.77 | 0.84 | 60 | NAD |
| 2 | 422 | 0.77 | 0.85 | 55 | NAD |
| 3 | 405 | 0.76 | 0.86 | 53 | NAD |
| 4 | 520 | 0.75 | 0.83 | 62 | NAD |
| 5 | 1126 | 0.74 | 0.77 | 96 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1689 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 1636 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 459 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 450 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 392 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3WLE · Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with NAD · the same entry in another collection · chain D against D, 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 A1X808
- Elsewhere: RCSB PDB 3WLE · PDBe 3WLE · UniProt A1X808
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