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1Y5R

The crystal structure of murine 11b-hydroxysteroid dehydrogenase complexed with corticosterone

Functional Information from GO Data
ChainGOidnamespacecontents
A0005496molecular_functionsteroid binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006704biological_processglucocorticoid biosynthetic process
A0006706biological_processsteroid catabolic process
A0006713biological_processglucocorticoid catabolic process
A0008202biological_processsteroid metabolic process
A0008212biological_processmineralocorticoid metabolic process
A0016491molecular_functionoxidoreductase activity
A0030324biological_processlung development
A0031965cellular_componentnuclear membrane
A0042803molecular_functionprotein homodimerization activity
A0043456biological_processregulation of pentose-phosphate shunt
A0045177cellular_componentapical part of cell
A0047022molecular_function7-beta-hydroxysteroid dehydrogenase (NADP+) activity
A0050661molecular_functionNADP binding
A0070524molecular_function11-beta-hydroxysteroid dehydrogenase (NADP+) activity
B0005496molecular_functionsteroid binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006704biological_processglucocorticoid biosynthetic process
B0006706biological_processsteroid catabolic process
B0006713biological_processglucocorticoid catabolic process
B0008202biological_processsteroid metabolic process
B0008212biological_processmineralocorticoid metabolic process
B0016491molecular_functionoxidoreductase activity
B0030324biological_processlung development
B0031965cellular_componentnuclear membrane
B0042803molecular_functionprotein homodimerization activity
B0043456biological_processregulation of pentose-phosphate shunt
B0045177cellular_componentapical part of cell
B0047022molecular_function7-beta-hydroxysteroid dehydrogenase (NADP+) activity
B0050661molecular_functionNADP binding
B0070524molecular_function11-beta-hydroxysteroid dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NDP A 1
ChainResidue
AC0R11
ATHR92
AMET93
AASN119
AILE121
AILE168
ASER169
ASER170
ATYR183
ALYS187
ALEU215
AGLY41
AGLY216
ALEU217
AILE218
ATHR220
ATHR222
AALA223
ASER43
ALYS44
AGLY45
AILE46
AALA65
AARG66
ASER67

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NDP B 2
ChainResidue
BC0R12
BGLY41
BSER43
BLYS44
BGLY45
BILE46
BARG66
BSER67
BTHR92
BMET93
BASN119
BHIS120
BILE121
BILE168
BSER169
BSER170
BTYR183
BLYS187
BLEU215
BGLY216
BLEU217
BILE218
BTHR220
BTHR222
BALA223

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE C0R A 11
ChainResidue
ANDP1
AILE121
ASER170
AGLN177
ATYR183
ATHR222

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE C0R B 12
ChainResidue
BNDP2
BILE121
BTHR124
BSER170
BGLN177
BILE180
BTYR183
BLEU217
BILE227

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkmtqpmIapYSASKFALdGFFsTIR
ChainResidueDetails
ASER170-ARG198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues68
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P28845","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS187
ASER170
ATYR183

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS187
BSER170
BTYR183

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS187
ASER170
ATYR183
AASN143

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS187
BSER170
BTYR183
BASN143

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS187
AILE180

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS187
BILE180

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS187
ATYR183

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS187
BTYR183

249697

PDB entries from 2026-02-25

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