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Site-directed mutagenesis on (serine) carboxypeptidase Y from yeast. the significance of thr 60 and met 398 in hydrolysis and aminolysis reactions
Analyse Site-directed mutagenesis on (serine) carboxypeptidase Y from yeast. the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CPY
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00729
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 421 | — | P00729 |
Compared structures
- 1CPY · Site-directed mutagenesis on (serine) carboxypeptidase Y from yeast. the significance of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00729 · AlphaFold monomer V2.0 prediction for carboxypeptidase Y (P00729) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P00729
- Elsewhere: RCSB PDB 1CPY · PDBe 1CPY · UniProt P00729
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