Research workbench
Cutinase, N172K, R196D mutant, monoclinic crystal form with three molecules per asymmetric unit
Analyse Cutinase, N172K, R196D mutant, monoclinic crystal form with three molecules per… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CUD
- Type
- protein
- Length
- 591 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase
- EC
- 3.1.1.3
- UniProt
- P00590
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Cutinase (EC 3.1.1.3) | protein | 197 | 43% helix, 16% strand | P00590 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.57 | 0.79 | 32 | empty |
| 2 | 90 | 0.41 | 0.78 | 25 | empty |
| 3 | 82 | 0.39 | 0.78 | 13 | empty |
| 4 | 79 | 0.30 | 0.73 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–B · 319 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 212 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1CUD · Cutinase, N172K, R196D mutant, monoclinic crystal form with three molecules per… · the same entry in another collection · chain A against A, TM-score 1.00
- P00590 · AlphaFold monomer V2.0 prediction for cutinase 1 (P00590) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P00590
- Elsewhere: RCSB PDB 1CUD · PDBe 1CUD · UniProt P00590
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