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3F1S

Crystal structure of Protein Z complexed with protein Z-dependent inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0007596biological_processblood coagulation
A0008201molecular_functionheparin binding
A0060046biological_processregulation of acrosome reaction
A0070062cellular_componentextracellular exosome
A0097421biological_processliver regeneration
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CsCaqGYrlgedhkqC
ChainResidueDetails
BCYS110-CYS125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20427285
ChainResidueDetails
BASN185
BASN292

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19528533, ECO:0000269|PubMed:20427285
ChainResidueDetails
BASN193

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN266

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20427285
ChainResidueDetails
AASN176

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:20427285
ChainResidueDetails
AASN274

219140

PDB entries from 2024-05-01

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