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

2VDY

Crystal structure of the reactive loop cleaved Corticosteroid Binding Globulin complexed with Cortisol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005496molecular_functionsteroid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006704biological_processglucocorticoid biosynthetic process
A0008211biological_processglucocorticoid metabolic process
A0008289molecular_functionlipid binding
A0070062cellular_componentextracellular exosome
A0140104molecular_functionmolecular carrier activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005496molecular_functionsteroid binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006704biological_processglucocorticoid biosynthetic process
B0008211biological_processglucocorticoid metabolic process
B0008289molecular_functionlipid binding
B0070062cellular_componentextracellular exosome
B0140104molecular_functionmolecular carrier activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HCY A1384
ChainResidue
ASER19
AGLN232
AILE263
AASN264
ASER267
AHIS368
ATRP371
AHOH2109

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HCY B1384
ChainResidue
BGLN232
BARG260
BASN264
BSER267
BHIS368
BTRP371
BSER19

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. LRFNQPFIImI
ChainResidueDetails
ALEU355-ILE365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18513745","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VDY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Conserved cysteine within steroid binding domain"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI7
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_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon