Research workbench
A novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site
Analyse A novel serine protease inhibition motif involving a multi-centered short… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GI0
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-trypsin
- EC
- 3.4.21.4
- UniProt
- P00760
- Ligands
- BMZ, CA, MG, SO4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-trypsin (EC 3.4.21.4) | protein | 223 | 10% helix, 35% strand | P00760 |
Ligands and binding sites
- BMZ · 2-(2-hydroxy-phenyl)-1H-benzoimidazole-5-carboxamidine · ligand · chains A
- CA · Calcium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1GI0 · A novel serine protease inhibition motif involving a multi-centered short hydrogen… · the same entry in another collection · 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 P00760
- Elsewhere: RCSB PDB 1GI0 · PDBe 1GI0 · UniProt P00760
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