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Trypsin with inhibitor aeruginosin 98-B

Analyse Trypsin with inhibitor aeruginosin 98-B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AQ7
Type: protein
Length: 225 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trypsin; Aeruginosin 98-B
EC: 3.4.21.4
UniProt: P00760
Ligands: 34H, AG2
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trypsin (EC 3.4.21.4)	protein	223	10% helix, 36% strand	P00760
B	Aeruginosin 98-B	protein	2	0% helix, 0% strand	—

Ligands and binding sites

34H · (2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoic acid · ligand · chains A, B
AG2 · Agmatine · ligand · chains A, B

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	55	0.38	0.80	19	empty

Interfaces

1 interface between chains.

A–B · 224 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 covalent, 1 d-amino, 1 modified (disulfide, covalent ligand, D-amino acid, nonstandard).

Compared structures

1AQ7 · Trypsin with inhibitor aeruginosin 98-B · 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 1AQ7 · PDBe 1AQ7 · UniProt P00760

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