Research workbench
Engineering enzyme sub-site specificity: preparation, kinetic characterization and X-ray analysis at 2.0-ångströms resolution of VAL111PHE site-mutated calf chymosin
Analyse Engineering enzyme sub-site specificity: preparation, kinetic characterization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CMS
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00794
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 320 | — | P00794 |
Compared structures
- 3CMS · Engineering enzyme sub-site specificity: preparation, kinetic characterization and X-ray… · the same entry in another collection · chain A against A, TM-score 1.00
- P00794 · AlphaFold monomer V2.0 prediction for chymosin (P00794) · 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 P00794
- Elsewhere: RCSB PDB 3CMS · PDBe 3CMS · UniProt P00794
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