Research workbench
The primary structure and structural characteristics of achromobacter lyticus protease I, a lysine-specific serine protease
Analyse The primary structure and structural characteristics of achromobacter lyticus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ARC
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Achromobacter protease I
- EC
- 3.4.21.50
- UniProt
- P15636
- Ligands
- TCK
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Achromobacter protease I (EC 3.4.21.50) | protein | 263 | 16% helix, 33% strand | P15636 |
Ligands and binding sites
- TCK · N-[(1S)-5-amino-1-(chloroacetyl)pentyl]-4-methylbenzenesulfonamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1ARC · The primary structure and structural characteristics of achromobacter lyticus protease I… · the same entry in another collection · chain A against A, TM-score 1.00
- P15636 · AlphaFold monomer V2.0 prediction for protease 1 (P15636) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P15636
- Elsewhere: RCSB PDB 1ARC · PDBe 1ARC · UniProt P15636
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