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6TE7

The structure of CYP121 in complex with inhibitor S2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0009975molecular_functioncyclase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0070025molecular_functioncarbon monoxide binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue N55 A 901
ChainResidue
ATHR77
AVAL228
AALA233
AHEM904
AVAL78
ASER163
AALA167
APHE168
AALA178
AASN181
ATRP182
AASP185

site_idAC2
Number of Residues4
Detailsbinding site for residue PGE A 902
ChainResidue
AALA288
ATHR289
ALYS301
AGLY302

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 903
ChainResidue
ALYS159
ALEU160
AARG184
AASP185
ATYR188
AHOH1008
AHOH1080
AHOH1338

site_idAC4
Number of Residues27
Detailsbinding site for residue HEM A 904
ChainResidue
AMET62
AMET86
AHIS146
APHE230
AALA233
AGLY234
ASER237
ATHR238
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
ALEU350
AGLY351
AN55901
AHOH1006
AHOH1045
AHOH1065
AHOH1166
AHOH1176
AHOH1231

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG
ChainResidueDetails
APHE338-GLY347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919
ChainResidueDetails
ASER237
ALYS301
AGLN385
ATHR77

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASN85

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594
ChainResidueDetails
AARG286
AHIS343

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS345

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Participates in a stacking interactions with the tyrosyl of cYY
ChainResidueDetails
ATRP182
APHE168

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for the position of heme
ChainResidueDetails
APRO346

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PDB entries from 2024-06-12

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