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3H5C

X-Ray Structure of Protein Z-Protein Z Inhibitor Complex

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
A0010466biological_processnegative regulation of peptidase activity
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_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CqDsiwgYtCtC
ChainResidueDetails
BCYS62-CYS73

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCspGyeGSnC
ChainResidueDetails
BCYS71-CYS82

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCspGYegsn....C
ChainResidueDetails
BCYS71-CYS82
BCYS110-CYS125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2244898
ChainResidueDetails
BPRO50
BCYS73
BGLY76
BGLU78
BGLU83
BCYS51
BGLN54
BHIS58
BGLY60
BGLN63
BASP64
BTYR69
BTHR70

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000250
ChainResidueDetails
BSER107

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201
ChainResidueDetails
BGLY96

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20427285
ChainResidueDetails
BLEU102
BGLU228
BPRO335

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19528533, ECO:0000269|PubMed:20427285
ChainResidueDetails
BALA236

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BMET309

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

224201

PDB entries from 2024-08-28

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