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3ZKP

Structure of a mutant of P450 EryK in complex with erythromycin B.

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
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 412
ChainResidue
AILE87
ATHR246
ALEU249
AMET291
AARG293
ASER345
APHE346
AGLY347
AHIS351
ACYS353
AGLY355
AHIS88
AALA359
AERB413
AHOH2067
AHOH2213
AHOH2289
AHOH2328
AHIS95
AARG99
APHE106
ALEU238
AALA241
AGLY242
ATHR245

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ERB A 413
ChainResidue
AHIS88
AGLU89
APRO177
AILE186
ALEU190
AALA237
ALEU240
AALA241
ATHR245
APHE288
AGLN292
AHEM412
AHOH2086
AHOH2212
AHOH2213
AHOH2248
AHOH2254
AHOH2329

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHFCLG
ChainResidueDetails
APHE346-GLY355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AHIS88
AHIS95
AARG99
AGLN292
AARG293
AHIS351

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS353

222624

PDB entries from 2024-07-17

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