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1PKF

Crystal Structure of Epothilone D-bound Cytochrome P450epoK

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
A0046872molecular_functionmetal ion binding
A0050814biological_processepothilone biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 440
ChainResidue
APHE62
ATHR259
ATHR305
AARG307
AALA357
ATYR358
AGLY359
AHIS363
ACYS365
APRO366
AGLY367
ALEU95
AEPD450
AHOH471
AHOH591
APHE96
AHIS103
AARG107
AILE251
AALA254
AGLY255
ATHR258

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE EPD A 450
ChainResidue
ALEU95
APHE96
AALA180
ALEU183
AGLY184
AVAL188
ATHR258
AGLY304
ATHR305
AALA402
APHE403
AHEM440
AHOH464
AHOH488
AHOH632

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12933799
ChainResidueDetails
AALA180
AGLY304

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:12933799
ChainResidueDetails
ACYS365

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AASP257
ATHR258

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PDB entries from 2025-02-05

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