Research workbench

Human anionic trypsin after autoproteolysis at ARG122

Analyse Human anionic trypsin after autoproteolysis at ARG122 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Z9F
Type: protein
Length: 446 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P07478
Ligands: CA

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X, A	—	protein	99	—	P07478
Y, B	—	protein	124	—	P07478

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains X, A

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

Compared structures

7Z9F · Human anionic trypsin after autoproteolysis at Arg122 · the same entry in another collection · chain X against X, TM-score 1.00
P07478 · AlphaFold monomer V2.0 prediction for trypsin-2 (P07478) · a predicted model of the same protein · chain Y 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 P07478
Elsewhere: RCSB PDB 7Z9F · PDBe 7Z9F · UniProt P07478

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