Structure of PDB 4wwy Chain B Binding Site BS01

Receptor Information

>4wwy Chain B (length=224) Species: 9606 (Homo sapiens)

IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRL
GEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINAHV
STISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEA
SYPGKITSNMFCVGFLEGGKDSCQRDSGGPVVCNGQLQGVVSWGDGCAQK
NKPGVYTKVYNYVKWIKNTIAANS

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 4wwy Chain B Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4wwy Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as Substrates.
• Resolution: 1.7 Å
• Binding residue (original residue number in PDB): H40 R66 E70 I73
• Binding residue (residue number reindexed from 1): H23 R49 E52 I55
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D102 Q192 R193 D194 S195 G196
• Catalytic site (residue number reindexed from 1): H40 D84 Q174 R175 D176 S177 G178
• Enzyme Commision number: 3.4.21.4: trypsin.

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis
• GO:0007586 digestion
• GO:0022617 extracellular matrix disassembly

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0062023 collagen-containing extracellular matrix
• GO:0072562 blood microparticle

External links

• PDB: RCSB:4wwy, PDBe:4wwy, PDBj:4wwy
• PDBsum: 4wwy
• PubMed: 26175157
• UniProt: P07477|TRY1_HUMAN Serine protease 1 (Gene Name=PRSS1)