Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1XU8

The 2.8 A structure of a tumour suppressing serpin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001533cellular_componentcornified envelope
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0009986cellular_componentcell surface
A0045177cellular_componentapical part of cell
B0001533cellular_componentcornified envelope
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0009986cellular_componentcell surface
B0045177cellular_componentapical part of cell
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3243
ChainResidue
ALYS109
BLYS173
BALA202
BTHR203

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 3244
ChainResidue
ALYS129
ALEU148
AASP150
AASN151
ASER152

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. LNADHPFIYiI
ChainResidueDetails
ALEU348-ILE358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reactive bond homolog","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon