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1Y5M

The crystal structure of murine 11b-hydroxysteroid dehydrogenase: an important therapeutic target for diabetes

Functional Information from GO Data
ChainGOidnamespacecontents
A0005496molecular_functionsteroid binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006704biological_processglucocorticoid biosynthetic process
A0006706biological_processsteroid catabolic process
A0006713biological_processglucocorticoid catabolic process
A0008202biological_processsteroid metabolic process
A0008212biological_processmineralocorticoid metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0030324biological_processlung development
A0031965cellular_componentnuclear membrane
A0042803molecular_functionprotein homodimerization activity
A0043231cellular_componentintracellular membrane-bounded organelle
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
A0102196molecular_functioncortisol dehydrogenase activity
B0005496molecular_functionsteroid binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006704biological_processglucocorticoid biosynthetic process
B0006706biological_processsteroid catabolic process
B0006713biological_processglucocorticoid catabolic process
B0008202biological_processsteroid metabolic process
B0008212biological_processmineralocorticoid metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0030324biological_processlung development
B0031965cellular_componentnuclear membrane
B0042803molecular_functionprotein homodimerization activity
B0043231cellular_componentintracellular membrane-bounded organelle
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
B0102196molecular_functioncortisol dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 293
ChainResidue
BGLY45
BARG48
BTHR220
BGLU221
BLYS238
BHOH312
BHOH341

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 294
ChainResidue
BARG48
BLYS73

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 293
ChainResidue
AGLY45
AARG48
ATHR220
AGLU221
ALYS238
AHOH327

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 294
ChainResidue
AARG48

site_idAC5
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NDP A 1
ChainResidue
AGLY41
AALA42
ASER43
ALYS44
AGLY45
AILE46
AALA65
AARG66
ASER67
AGLY91
ATHR92
AMET93
AASN119
AILE121
AILE168
ASER169
ASER170
ATYR183
ALYS187
ALEU215
AGLY216
ALEU217
AILE218
ATHR220
ATHR222
AALA223
AHOH312
AHOH325
AHOH327
AHOH330
AHOH337
AHOH341

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP B 2
ChainResidue
BGLY41
BALA42
BSER43
BLYS44
BGLY45
BILE46
BALA65
BARG66
BSER67
BTHR92
BMET93
BASN119
BHIS120
BILE121
BILE168
BSER169
BSER170
BTYR183
BLYS187
BLEU215
BGLY216
BLEU217
BILE218
BTHR220
BTHR222
BALA223
BHOH341

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OCT A 301
ChainResidue
AGLN177
BSER280

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OCT B 302
ChainResidue
BGLN177

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ASER184
BSER184

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AHIS120
ALEU171
ASER184
BALA42
BMET93
BHIS120
BLEU171
BSER184
AALA42
AMET93

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P28845
ChainResidueDetails
AASP219
BASP219

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BGLY163
BVAL208
AGLY163
AVAL208

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PDB entries from 2024-06-12

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