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6UEZ

Human sterol 14a-demethylase (CYP51) in complex with the substrate lanosterol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue HEM A 601
ChainResidue
ATYR131
APRO441
APHE442
AGLY443
AHIS447
AARG448
ACYS449
AALA455
AHOH741
AHOH798
ATYR145
APHE152
AALA311
ATHR315
APRO376
AILE377
AMET380
AARG382

site_idAC2
Number of Residues11
Detailsbinding site for residue LAN A 602
ChainResidue
ATYR131
APHE139
ATYR145
APHE152
ALEU159
AGLY303
ALEU310
AALA311
AILE377
AILE379
AHOH786

site_idAC3
Number of Residues19
Detailsbinding site for residue HEM B 601
ChainResidue
BTYR131
BTYR145
BPHE152
BALA311
BTHR315
BPRO376
BILE377
BMET380
BARG382
BPRO441
BPHE442
BGLY443
BHIS447
BCYS449
BILE450
BGLY451
BALA455
BLAN602
BHOH799

site_idAC4
Number of Residues11
Detailsbinding site for residue LAN B 602
ChainResidue
BTYR131
BVAL143
BTYR145
BPHE152
BLEU159
BPHE234
BLEU310
BILE377
BILE379
BHEM601
BHOH764

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGRHRCIG
ChainResidueDetails
APHE442-GLY451

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTASHC
ChainResidueDetails
ALEU204-CYS209

site_idPS00626
Number of Residues11
DetailsRCC1_2 Regulator of chromosome condensation (RCC1) signature 2. LAGGfSHAAWL
ChainResidueDetails
ALEU230-LEU240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:20149798
ChainResidueDetails
AALA455
BALA455

219140

PDB entries from 2024-05-01

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