Research workbench

Crystal structure of anionic trypsin isoform 1 from chum salmon

Analyse Crystal structure of anionic trypsin isoform 1 from chum salmon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZPQ
Type: protein
Length: 440 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anionic trypsin
UniProt: Q8AV11
Ligands: BEN, CA, SO4
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Anionic trypsin	protein	220	10% helix, 35% strand	Q8AV11

Ligands and binding sites

BEN · Benzamidine · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	413	0.64	0.78	41	empty

Interfaces

1 interface between chains.

A–B · 283 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

2ZPQ · Crystal structure of anionic trypsin isoform 1 from chum salmon · the same entry in another collection · 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 Q8AV11
Elsewhere: RCSB PDB 2ZPQ · PDBe 2ZPQ · UniProt Q8AV11

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.