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6TEV

The structure of CYP121 in complex with inhibitor L44

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 Residues11
Detailsbinding site for residue N5W A 901
ChainResidue
AMET62
AN5W902
AHEM905
ATHR65
AASN74
ALEU76
AVAL82
AVAL83
AASN85
ATHR229
APRO285

site_idAC2
Number of Residues15
Detailsbinding site for residue N5W A 902
ChainResidue
AVAL78
ALEU164
AALA167
APHE168
ATRP182
AASP185
AVAL228
AARG386
AN5W901
AHEM905
AHOH1028
AHOH1063
AHOH1080
AHOH1129
AHOH1262

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 903
ChainResidue
ASER248
AGLN251
AARG252
AILE276
AHOH1022

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 904
ChainResidue
ASER216
AASP220
AASP328
APRO330
AHOH1076

site_idAC5
Number of Residues23
Detailsbinding site for residue HEM A 905
ChainResidue
AMET62
AMET86
AHIS146
AGLY234
ASER237
APHE241
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
AN5W901
AN5W902
AHOH1023
AHOH1080
AHOH1101
AHOH1187
AHOH1201

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
ATHR77
ASER237
ALYS301
AGLN385

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
APHE168
ATRP182

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

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PDB entries from 2024-09-11

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