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5OP9

The crystal structure of P450 CYP121 in complex with lead compound 7e

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 Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH515

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH527
AHOH792
AHOH796
ASER12
AARG17

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH551
AHOH570
AHOH578

site_idAC4
Number of Residues22
Detailsbinding site for residue HEM A 404
ChainResidue
AMET62
AMET86
AHIS146
AGLY234
ASER237
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
ABZ6405
ASO4406
AHOH537
AHOH541
AHOH565
AHOH583
AHOH658
AHOH754

site_idAC5
Number of Residues15
Detailsbinding site for residue BZ6 A 405
ChainResidue
ATHR77
AVAL78
AVAL82
AASN85
AALA167
APHE168
ATRP182
AVAL228
ATHR229
AHEM404
AHOH540
AHOH563
AHOH709
AHOH754
AHOH822

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 406
ChainResidue
AARG386
AHEM404
AHOH565
AHOH721

site_idAC7
Number of Residues8
Detailsbinding site for residue SO4 A 407
ChainResidue
AARG134
AASN135
APHE161
ASER165
AARG381
AARG391
AHOH522
AHOH642

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 A 408
ChainResidue
ASER219
AARG252
ASER324
AILE325
AHOH650
AHOH824

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

220472

PDB entries from 2024-05-29

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