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Engineering inhibitors highly selective for the S1 sites of SER190 trypsin-like serine protease drug targets

Analyse Engineering inhibitors highly selective for the S1 sites of SER190 trypsin-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GJ6
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: 132, CA
Pockets: 1 · best druggability 0.38

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

132 · 6-chloro-2-(2-hydroxy-biphenyl-3-yl)-1H-indole-5-carboxamidine · ligand · chains A
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.38	0.81	16	132

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1GJ6 · Engineering inhibitors highly selective for the S1 sites of SER190 trypsin-like serine… · 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 1GJ6 · PDBe 1GJ6 · UniProt P00760

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