4C49
Reactive loop cleaved human CBG in complex with cortisol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
A | 0005496 | molecular_function | steroid binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006704 | biological_process | glucocorticoid biosynthetic process |
A | 0008211 | biological_process | glucocorticoid metabolic process |
A | 0008289 | molecular_function | lipid binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0140104 | molecular_function | molecular carrier activity |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
B | 0005496 | molecular_function | steroid binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006704 | biological_process | glucocorticoid biosynthetic process |
B | 0008211 | biological_process | glucocorticoid metabolic process |
B | 0008289 | molecular_function | lipid binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0140104 | molecular_function | molecular carrier activity |
C | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
C | 0005496 | molecular_function | steroid binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0006704 | biological_process | glucocorticoid biosynthetic process |
C | 0008211 | biological_process | glucocorticoid metabolic process |
C | 0008289 | molecular_function | lipid binding |
C | 0070062 | cellular_component | extracellular exosome |
C | 0140104 | molecular_function | molecular carrier activity |
D | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
D | 0005496 | molecular_function | steroid binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0006704 | biological_process | glucocorticoid biosynthetic process |
D | 0008211 | biological_process | glucocorticoid metabolic process |
D | 0008289 | molecular_function | lipid binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 0140104 | molecular_function | molecular carrier activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE HCY A 1384 |
Chain | Residue |
A | GLN232 |
A | ARG260 |
A | ILE263 |
A | ASN264 |
A | SER267 |
A | HIS368 |
A | TRP371 |
D | SER165 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE HCY B 1384 |
Chain | Residue |
B | GLN232 |
B | ARG260 |
B | ILE263 |
B | ASN264 |
B | SER267 |
B | HIS368 |
B | TRP371 |
B | SER19 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HCY C 1384 |
Chain | Residue |
B | LEU167 |
C | SER19 |
C | GLN232 |
C | ARG260 |
C | ILE263 |
C | ASN264 |
C | PHE366 |
C | HIS368 |
C | TRP371 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HCY D 1384 |
Chain | Residue |
A | GLN139 |
A | ASP140 |
D | SER19 |
D | GLN232 |
D | THR240 |
D | ARG260 |
D | ILE263 |
D | ASN264 |
D | PHE366 |
D | TRP371 |
D | HOH2004 |
Functional Information from PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. LRFNQPFIImI |
Chain | Residue | Details |
A | LEU355-ILE365 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18513745","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VDY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Site: {"description":"Conserved cysteine within steroid binding domain"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"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_FI5 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
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_FI8 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |