Research workbench
Cut-1A; ncn-pt-pincer-cutinase hybrid
Analyse Cut-1A; ncn-pt-pincer-cutinase hybrid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EF3
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase-1
- EC
- 3.1.1.74
- UniProt
- P00590
- Ligands
- NXC
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase-1 (EC 3.1.1.74) | protein | 196 | 44% helix, 15% strand | P00590 |
Ligands and binding sites
- NXC · (2,6-bis[(dimethylamino-kappaN)methyl]-4-{3-[(S)-ethoxy(4-nitrophenoxy)phosphoryl]propyl}phenyl-kappaC~1~)(chloro)platinum(2+) · 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 3EF3 · PDBe 3EF3 · UniProt P00590
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