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4YMK

Crystal Structure of Stearoyl-Coenzyme A Desaturase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004768molecular_functionstearoyl-CoA 9-desaturase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006636biological_processunsaturated fatty acid biosynthetic process
A0006641biological_processtriglyceride metabolic process
A0007584biological_processresponse to nutrient
A0008610biological_processlipid biosynthetic process
A0009617biological_processresponse to bacterium
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A0032896molecular_functionpalmitoyl-CoA 9-desaturase activity
A0042632biological_processcholesterol homeostasis
A0046872molecular_functionmetal ion binding
A0048733biological_processsebaceous gland development
A0050830biological_processdefense response to Gram-positive bacterium
A0050872biological_processwhite fat cell differentiation
A0050873biological_processbrown fat cell differentiation
A0055088biological_processlipid homeostasis
A0055092biological_processsterol homeostasis
A0070542biological_processresponse to fatty acid
A0120162biological_processpositive regulation of cold-induced thermogenesis
A1903699biological_processtarsal gland development
A1903966biological_processmonounsaturated fatty acid biosynthetic process
D0004768molecular_functionstearoyl-CoA 9-desaturase activity
D0005506molecular_functioniron ion binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0006636biological_processunsaturated fatty acid biosynthetic process
D0006641biological_processtriglyceride metabolic process
D0007584biological_processresponse to nutrient
D0008610biological_processlipid biosynthetic process
D0009617biological_processresponse to bacterium
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
D0032896molecular_functionpalmitoyl-CoA 9-desaturase activity
D0042632biological_processcholesterol homeostasis
D0046872molecular_functionmetal ion binding
D0048733biological_processsebaceous gland development
D0050830biological_processdefense response to Gram-positive bacterium
D0050872biological_processwhite fat cell differentiation
D0050873biological_processbrown fat cell differentiation
D0055088biological_processlipid homeostasis
D0055092biological_processsterol homeostasis
D0070542biological_processresponse to fatty acid
D0120162biological_processpositive regulation of cold-induced thermogenesis
D1903699biological_processtarsal gland development
D1903966biological_processmonounsaturated fatty acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS116
AHIS121
AHIS153
AHIS157
AHIS297

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AHOH542
AHIS156
AHIS265
AHIS294
AHIS298

site_idAC3
Number of Residues25
Detailsbinding site for residue ST9 A 403
ChainResidue
AASN71
AILE111
ATHR112
AHIS116
APHE142
AGLN143
AASN144
ATRP149
AARG151
AASP152
AHIS153
ATRP180
ALEU181
AVAL183
AARG184
ALYS185
AVAL189
AGLY193
AGLY194
AARG211
ATHR257
ATRP258
AVAL260
AASN261
AALA288

site_idAC4
Number of Residues5
Detailsbinding site for residue MPG A 404
ChainResidue
AGLY100
ATYR104
AMET105
ALEU286
AVAL289

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN D 401
ChainResidue
DHIS116
DHIS121
DHIS153
DHIS157
DHIS297

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN D 402
ChainResidue
DHIS156
DHIS265
DHIS294
DHIS298
DHOH530

site_idAC7
Number of Residues27
Detailsbinding site for residue ST9 D 403
ChainResidue
DASN71
DILE111
DTHR112
DHIS116
DPHE142
DGLN143
DASN144
DTRP149
DARG151
DASP152
DHIS153
DTRP180
DLEU181
DVAL183
DARG184
DLYS185
DVAL189
DLYS190
DGLY193
DGLY194
DLEU254
DTHR257
DTRP258
DASN261
DGLY287
DALA288
DHOH519

site_idAC8
Number of Residues4
Detailsbinding site for residue MPG D 404
ChainResidue
DGLY100
DTYR104
DMET105
DLEU286

Functional Information from PROSITE/UniProt
site_idPS00476
Number of Residues15
DetailsFATTY_ACID_DESATUR_1 Fatty acid desaturases family 1 signature. GEgFHNYHHtFPfDY
ChainResidueDetails
AGLY290-TYR304

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26098370","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"26098370","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues196
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26098370","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues95
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16275639","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsMotif: {"description":"Histidine box-1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsMotif: {"description":"Histidine box-2","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsMotif: {"description":"Histidine box-3","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26098370","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26098370","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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