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1STF

THE REFINED 2.4 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF RECOMBINANT HUMAN STEFIN B IN COMPLEX WITH THE CYSTEINE PROTEINASE PAPAIN: A NOVEL TYPE OF PROTEINASE INHIBITOR INTERACTION

Functional Information from GO Data
ChainGOidnamespacecontents
E0006508biological_processproteolysis
E0008234molecular_functioncysteine-type peptidase activity
I0002020molecular_functionprotease binding
I0003723molecular_functionRNA binding
I0004866molecular_functionendopeptidase inhibitor activity
I0004869molecular_functioncysteine-type endopeptidase inhibitor activity
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005634cellular_componentnucleus
I0005730cellular_componentnucleolus
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0008344biological_processadult locomotory behavior
I0030414molecular_functionpeptidase inhibitor activity
I0031012cellular_componentextracellular matrix
I0034774cellular_componentsecretory granule lumen
I0045861biological_processnegative regulation of proteolysis
I0070062cellular_componentextracellular exosome
I1904724cellular_componenttertiary granule lumen
I1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfSA
ChainResidueDetails
EGLN19-ALA30

site_idPS00287
Number of Residues14
DetailsCYSTATIN Cysteine proteases inhibitors signature. SQVVAGTNYfIKVH
ChainResidueDetails
ISER52-HIS65

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG
ChainResidueDetails
EVAL157-GLY167

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiKNSWgtgWGenGYIrI
ChainResidueDetails
ETYR170-ILE189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive site
ChainResidueDetails
IGLY9

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
IMET6

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:5681232, ECO:0000269|PubMed:6502713, ECO:0000269|PubMed:952885, ECO:0007744|PDB:1PAD, ECO:0007744|PDB:9PAP
ChainResidueDetails
EASN175

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: covalent => ECO:0000269|PubMed:8416808, ECO:0007744|PDB:1POP
ChainResidueDetails
ECCS25

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
EASN175
EHIS159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
EGLN19
EHIS159

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
EASN175
EGLN19
EHIS159

site_idMCSA1
Number of Residues4
DetailsM-CSA 174
ChainResidueDetails

237735

PDB entries from 2025-06-18

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