Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1Q5D

Epothilone B-bound Cytochrome P450epoK

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
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
ALEU95
ATHR259
ATHR305
AARG307
AALA357
ATYR358
AHIS363
ACYS365
APRO366
AGLY367
AALA371
APHE96
AEPB450
AHOH451
AHOH453
AHIS103
AARG107
APHE114
AILE251
AALA254
AGLY255
ATHR258

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE EPB A 450
ChainResidue
AARG71
APHE96
AALA180
ALEU183
AGLY184
ATHR258
ALEU301
AGLY304
ATHR305
AALA402
APHE403
AHEM440
AHOH451
AHOH460
AHOH466
AHOH680

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12933799","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12933799","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon