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
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005634 | cellular_component | nucleus |
A | 0006953 | biological_process | acute-phase response |
A | 0006954 | biological_process | inflammatory response |
A | 0019216 | biological_process | regulation of lipid metabolic process |
A | 0030277 | biological_process | maintenance of gastrointestinal epithelium |
A | 0030414 | molecular_function | peptidase inhibitor activity |
A | 0031012 | cellular_component | extracellular matrix |
A | 0031093 | cellular_component | platelet alpha granule lumen |
A | 0034097 | biological_process | response to cytokine |
A | 0034774 | cellular_component | secretory granule lumen |
A | 0035578 | cellular_component | azurophil granule lumen |
A | 0070062 | cellular_component | extracellular exosome |
A | 0072562 | cellular_component | blood microparticle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 401 |
Chain | Residue |
A | THR203 |
A | GLN205 |
A | ASP303 |
A | HOH567 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | ASN30 |
A | SER95 |
A | PHE96 |
A | HOH611 |
B | SER387 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | HIS98 |
A | ARG101 |
A | GLN105 |
A | SER106 |
A | HOH592 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | GLU122 |
A | LEU124 |
A | ALA144 |
Functional Information from PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. VRFNRPFLMiI |
Chain | Residue | Details |
B | VAL370-ILE380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | DNA binding: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Glycosylation: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Glycosylation: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |