Research workbench
Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
Analyse Contribution of cutinase serine 42 side chain to the stabilization of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FFC
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase
- EC
- 3.1.1.3
- UniProt
- P00590
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase (EC 3.1.1.3) | protein | 197 | 44% helix, 16% strand | P00590 |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1FFC · Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion… · 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 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 P00590
- Elsewhere: RCSB PDB 1FFC · PDBe 1FFC · UniProt P00590
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.