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4ZYO

Crystal Structure of Human Integral Membrane Stearoyl-CoA Desaturase with Substrate

Functional Information from GO Data
ChainGOidnamespacecontents
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS120
AHIS125
AHIS157
AHIS161
AHIS301

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AHOH501
AHIS160
AHIS269
AHIS298
AHIS302

site_idAC3
Number of Residues31
Detailsbinding site for residue ST9 A 403
ChainResidue
AVAL72
AASN75
AALA112
AILE115
ATHR116
AHIS120
APHE146
AGLN147
AASN148
ATRP153
AARG155
AASP156
AHIS157
AHIS171
ATRP184
ALEU185
AVAL187
AARG188
ALYS189
AVAL193
ALYS194
AGLY197
AARG215
ATYR254
ATHR261
ATRP262
AVAL264
AASN265
AALA292
AVAL293
AGLU295

site_idAC4
Number of Residues7
Detailsbinding site for residue LMT A 404
ChainResidue
AALA60
AASP61
AALA62
AHIS167
AHIS190
AGLU195
ALYS196

Functional Information from PROSITE/UniProt
site_idPS00476
Number of Residues15
DetailsFATTY_ACID_DESATUR_1 Fatty acid desaturases family 1 signature. GEgFHNYHHsFPyDY
ChainResidueDetails
AGLY294-TYR308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26098317
ChainResidueDetails
ATRP73-ILE93
APHE98-GLY118
ATYR218-PHE237
APHE242-LEU263

site_idSWS_FT_FI2
Number of Residues6
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:26098317
ChainResidueDetails
APRO94-LYS97
ATRP238-THR241

site_idSWS_FT_FI3
Number of Residues193
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:26098317
ChainResidueDetails
AALA119-TYR217
AVAL264-GLY359

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:26098317
ChainResidueDetails
AASN75
AASN148
AARG155
AASP156
AARG188
ALYS189
ATRP262

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:26098317
ChainResidueDetails
AHIS120
AHIS125
AHIS157
AHIS160
AHIS161
AHIS269
AHIS298
AHIS301
AHIS302

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER198

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER203

223166

PDB entries from 2024-07-31

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