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6HGN

Crystal structure of Alpha1-antichymotrypsin variant DBS-II-allo-L55V: an allosterically controlled doxorubicin-binding serpin with an unprecedentedly high ligand release efficacy

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0006953biological_processacute-phase response
A0006954biological_processinflammatory response
A0019216biological_processregulation of lipid metabolic process
A0030277biological_processmaintenance of gastrointestinal epithelium
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0031093cellular_componentplatelet alpha granule lumen
A0034097biological_processresponse to cytokine
A0034774cellular_componentsecretory granule lumen
A0035578cellular_componentazurophil granule lumen
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 401
ChainResidue
ATHR203
AGLN205
AASP303
AHOH567

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 402
ChainResidue
AASN30
ASER95
APHE96
AHOH611
BSER387

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AHIS98
AARG101
AGLN105
ASER106
AHOH592

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU122
ALEU124
AALA144

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VRFNRPFLMiI
ChainResidueDetails
BVAL370-ILE380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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