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4AFX

Crystal structure of the reactive loop cleaved ZPI in I2 space group

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
A0007599biological_processhemostasis
A0008201molecular_functionheparin binding
A0030414molecular_functionpeptidase inhibitor activity
A0060046biological_processregulation of acrosome reaction
A0070062cellular_componentextracellular exosome
A0097421biological_processliver regeneration
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 1387
ChainResidue
AGLU292

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 1388
ChainResidue
AASN159
AARG163

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1389
ChainResidue
ASER64
AARG67

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1390
ChainResidue
ALEU120
APRO121
AGLU100
ALYS104
APRO117
AGLY118

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 1391
ChainResidue
AGLN102

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1392
ChainResidue
AHIS73
AGLY75
AASN76
AGLN323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Essential for interaction with PROZ => ECO:0000250
ChainResidueDetails
ATYR240
AASP293

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Reactive bond => ECO:0000250
ChainResidueDetails
AARG387

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER35

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN15

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN159

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20427285
ChainResidueDetails
AASN176

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:20427285
ChainResidueDetails
AASN274

218853

PDB entries from 2024-04-24

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