MolNFT v1 · #33777 · protein
Cutinase, a lipolytic enzyme with a preformed oxyanion hole
2CUT: “Cutinase, a lipolytic enzyme with a preformed oxyanion hole”. X-ray diffraction, 1 ligand (DEP). MolNFT v1 #33777 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2CUT
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase
- EC
- 3.1.1.-
- UniProt
- P00590
- Ligands
- DEP
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase (EC 3.1.1.-) | protein | 198 | 44% helix, 15% strand | P00590 |
Ligands and binding sites
- DEP · Diethyl phosphonate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).
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 P00590
- Elsewhere: RCSB PDB 2CUT · PDBe 2CUT · UniProt P00590
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