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6C94

Structure Of Cytochrome P450 4B1 (CYP4B1) Complexed with the Inhibitor HET0016

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0070330molecular_functionaromatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 600
ChainResidue
ALYS105
AVAL378
APRO440
APHE441
AARG446
AASN447
ACYS448
AGLY450
APHE453
AALA454
AMET458
ATYR110
AV16601
AHOH703
AHOH704
ALEU121
ATRP129
AARG133
APHE140
AGLU310
AGLY311
AVAL375

site_idAC2
Number of Residues7
Detailsbinding site for residue V16 A 601
ChainResidue
AVAL109
APHE309
AGLU310
ATHR314
AGLN377
AVAL486
AHEM600

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSaGPRNCIG
ChainResidueDetails
APHE441-GLY450

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: covalent => ECO:0000250|UniProtKB:P51869
ChainResidueDetails
AGLU310

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P51869
ChainResidueDetails
ACYS448

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P20816
ChainResidueDetails
ASER431

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PDB entries from 2024-06-12

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