Research workbench
Structure of carbonyl reductase CPCR2 from candida parapsilosis in complex with NADH
Analyse Structure of carbonyl reductase CPCR2 from candida parapsilosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C4O
- Type
- protein
- Length
- 1,233 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonyl reductase CPCR2
- EC
- 1.1.1.1
- UniProt
- O42703
- Ligands
- NAD, ZN
- Pockets
- 14 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonyl reductase CPCR2 (EC 1.1.1.1) | protein | 326 | 28% helix, 30% strand | O42703 |
| B | Carbonyl reductase CPCR2 (EC 1.1.1.1) | protein | 335 | 31% helix, 30% strand | O42703 |
| C | Carbonyl reductase CPCR2 (EC 1.1.1.1) | protein | 302 | 30% helix, 25% strand | O42703 |
| D | Carbonyl reductase CPCR2 (EC 1.1.1.1) | protein | 270 | 29% helix, 24% strand | O42703 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 9 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 578 | 0.77 | 0.83 | 65 | NAD |
| 2 | 685 | 0.70 | 0.77 | 70 | ZN |
| 3 | 628 | 0.69 | 0.78 | 44 | empty |
| 4 | 415 | 0.67 | 0.80 | 36 | empty |
| 5 | 348 | 0.65 | 0.80 | 46 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1543 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1507 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 653 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 625 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 516 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4C4O · Structure of carbonyl reductase CPCR2 from Candida parapsilosis in complex with NADH · 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 O42703
- Elsewhere: RCSB PDB 4C4O · PDBe 4C4O · UniProt O42703
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