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3LE2

Structure of Arabidopsis AtSerpin1. Native Stressed Conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0030414molecular_functionpeptidase inhibitor activity
A0048046cellular_componentapoplast
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 392
ChainResidue
ASER213
AHOH636
ATYR215
ATYR215
AASP216
AHOH405
AHOH420
AHOH447
AHOH452
AHOH594

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 393
ChainResidue
ASER235
ATYR237
APRO266
AHOH563
AHOH650

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 394
ChainResidue
AGLY89
APRO90
ALYS174
AGLY175
ATHR176
AHOH633

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 395
ChainResidue
ASER344
AGLY346
AVAL347
AILE348
ALYS349

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FVADHPFLLvV
ChainResidueDetails
APHE362-VAL372

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsRegion: {"description":"RCL"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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