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6WF2

Crystal structure of mouse SCD1 with a diiron center

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
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
A0016215molecular_functionacyl-CoA desaturase activity
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
B0004768molecular_functionstearoyl-CoA 9-desaturase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006636biological_processunsaturated fatty acid biosynthetic process
B0006641biological_processtriglyceride metabolic process
B0007584biological_processresponse to nutrient
B0008610biological_processlipid biosynthetic process
B0009617biological_processresponse to bacterium
B0016020cellular_componentmembrane
B0016215molecular_functionacyl-CoA desaturase activity
B0016491molecular_functionoxidoreductase activity
B0016717molecular_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
B0032896molecular_functionpalmitoyl-CoA 9-desaturase activity
B0042632biological_processcholesterol homeostasis
B0046872molecular_functionmetal ion binding
B0048733biological_processsebaceous gland development
B0050830biological_processdefense response to Gram-positive bacterium
B0050872biological_processwhite fat cell differentiation
B0050873biological_processbrown fat cell differentiation
B0055088biological_processlipid homeostasis
B0055092biological_processsterol homeostasis
B0070542biological_processresponse to fatty acid
B0120162biological_processpositive regulation of cold-induced thermogenesis
B1903699biological_processtarsal gland development
B1903966biological_processmonounsaturated fatty acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE A 401
ChainResidue
AHIS116
AHIS121
AHIS153
AHIS157
AHIS297

site_idAC2
Number of Residues4
Detailsbinding site for residue FE A 402
ChainResidue
AHIS156
AHIS265
AHIS294
AHIS298

site_idAC3
Number of Residues25
Detailsbinding site for residue 3VV A 403
ChainResidue
AASN71
AILE111
APHE142
AGLN143
AASN144
ATRP149
AARG151
AASP152
AHIS153
ATRP180
ALEU181
AVAL183
AARG184
ALYS185
AVAL189
ALYS190
AGLY193
AGLY194
ATYR250
ALEU254
ATHR257
ATRP258
AVAL260
AASN261
AALA288

site_idAC4
Number of Residues5
Detailsbinding site for residue FE B 401
ChainResidue
BHIS116
BHIS121
BHIS153
BHIS157
BHIS297

site_idAC5
Number of Residues4
Detailsbinding site for residue FE B 402
ChainResidue
BHIS156
BHIS265
BHIS294
BHIS298

site_idAC6
Number of Residues30
Detailsbinding site for residue 3VV B 403
ChainResidue
BASN71
BALA108
BILE111
BTHR112
BHIS116
BPHE142
BGLN143
BASN144
BGLU148
BTRP149
BARG151
BASP152
BHIS153
BTRP180
BLEU181
BVAL183
BARG184
BLYS185
BVAL189
BLYS190
BGLY193
BGLY194
BTYR250
BTHR257
BTRP258
BVAL260
BASN261
BGLY287
BALA288
BGLU291

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
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26098370
ChainResidueDetails
ATRP69-VAL89
ALEU94-GLY114
ATYR214-CYS233
APHE238-LEU259
BTRP69-VAL89
BLEU94-GLY114
BTYR214-CYS233
BPHE238-LEU259

site_idSWS_FT_FI2
Number of Residues12
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:26098370
ChainResidueDetails
APRO90-LYS93
ATRP234-THR237
BPRO90-LYS93
BTRP234-THR237

site_idSWS_FT_FI3
Number of Residues196
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:26098370
ChainResidueDetails
AALA115-TYR213
BALA115-TYR213

site_idSWS_FT_FI4
Number of Residues190
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:16275639
ChainResidueDetails
AVAL260-SER355
BVAL260-SER355

site_idSWS_FT_FI5
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:26098370
ChainResidueDetails
AASN71
BARG151
BASP152
BARG184
BLYS185
BTRP258
AASN144
AARG151
AASP152
AARG184
ALYS185
ATRP258
BASN71
BASN144

site_idSWS_FT_FI6
Number of Residues18
DetailsBINDING: BINDING => ECO:0000305|PubMed:26098370
ChainResidueDetails
AHIS116
BHIS116
BHIS121
BHIS153
BHIS156
BHIS157
BHIS265
BHIS294
BHIS297
BHIS298
AHIS121
AHIS153
AHIS156
AHIS157
AHIS265
AHIS294
AHIS297
AHIS298

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PDB entries from 2024-07-10

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