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2VDX

Crystal Structure of the reactive loop Cleaved Corticosteroid Binding Globulin

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A1384
ChainResidue
ATYR235
AGLY237
AHOH2058
AHOH2098
AHOH2099
AHOH2101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A1385
ChainResidue
AHOH2084
ASER215
ASER216
AHOH2079

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B1384
ChainResidue
BTYR235
BGLY237
BHOH2023
BHOH2085
BHOH2086

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A1386
ChainResidue
ALEU93
ALYS96
AHOH2029

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

243531

PDB entries from 2025-10-22

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