Research workbench
Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C
Analyse Structure-based prediction of modifications in glutarylamidase to allow… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GK1
- Type
- protein
- Length
- 1,350 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O86089
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 153 | — | O86089 |
| B, D | — | protein | 522 | — | O86089 |
Compared structures
- 1GK1 · Structure-based prediction of modifications in glutarylamidase to allow single-step… · the same entry in another collection · chain D against D, TM-score 1.00
- 1GK0 · Structure-based prediction of modifications in glutarylamidase to allow single-step… · an experimental structure of the same protein · chain B against B, 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 O86089
- Elsewhere: RCSB PDB 1GK1 · PDBe 1GK1 · UniProt O86089 · AlphaFold DB O86089
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