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4AJU

Crystal structure of the reactive loop cleaved ZPI in P41 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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1387
ChainResidue
AGLN102
AARG337
AARG338

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1388
ChainResidue
ASER64
AARG67
ALYS149
AARG175
ALYS208

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1389
ChainResidue
ALYS198
AARG364
APRO197

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1390
ChainResidue
ALYS253
AASN311

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1391
ChainResidue
ALEU222
ATHR223
APHE225
APRO270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Essential for interaction with PROZ","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20427285","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20427285","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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