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6TET

The structure of CYP121 in complex with inhibitor L21

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 Residues5
Detailsbinding site for residue EDO A 501
ChainResidue
ASER216
AASP220
AASP328
APRO330
AHOH647

site_idAC2
Number of Residues13
Detailsbinding site for residue N5Z A 502
ChainResidue
AALA178
AASN181
ATRP182
ATHR229
APHE280
AARG386
AEDO503
AHEM509
AHOH692
ATHR77
AVAL78
AALA167
APHE168

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
AVAL83
AN5Z502
AHEM509
AHOH601
AHOH875
AHOH957

site_idAC4
Number of Residues6
Detailsbinding site for residue PGE A 504
ChainResidue
AVAL5
AALA288
ATHR289
ALYS301
AGLY302
AHOH1003

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 505
ChainResidue
ATHR27
AASP296
AHOH960

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 506
ChainResidue
ASER248
AGLN251
AARG252
AILE276
AHOH640

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 507
ChainResidue
ALYS63
AGLU64

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 508
ChainResidue
ALEU160
AARG184
AASP185

site_idAC9
Number of Residues22
Detailsbinding site for residue HEM A 509
ChainResidue
AMET62
AMET86
AHIS146
AGLY234
ASER237
APHE241
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AN5Z502
AEDO503
AHOH646
AHOH692
AHOH701
AHOH713
AHOH786

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

221051

PDB entries from 2024-06-12

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