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3EL3

Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0010333molecular_functionterpene synthase activity
A0010334molecular_functionsesquiterpene synthase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016829molecular_functionlyase activity
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0042181biological_processketone biosynthetic process
A0046872molecular_functionmetal ion binding
A0051762biological_processsesquiterpene biosynthetic process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005829cellular_componentcytosol
B0010333molecular_functionterpene synthase activity
B0010334molecular_functionsesquiterpene synthase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016829molecular_functionlyase activity
B0017000biological_processantibiotic biosynthetic process
B0020037molecular_functionheme binding
B0042181biological_processketone biosynthetic process
B0046872molecular_functionmetal ion binding
B0051762biological_processsesquiterpene biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AASN108
AARG408
ALYS409
ACYS410
ASER412
ASER416
AILE271
AGLY275
ATHR278
AILE279
ATHR282
AARG343
APRO402
APHE403

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EL3 A 501
ChainResidue
ATRP92
APRO274
AVAL338
AILE447
ATHR448

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EL3 A 502
ChainResidue
ALEU91
ATRP339

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BASN108
BILE271
BGLY275
BTHR278
BILE279
BTHR282
BLEU341
BARG343
BPRO402
BSER404
BLYS407
BARG408
BLYS409
BCYS410
BSER412
BSER416
BEL3501

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EL3 B 501
ChainResidue
BTRP92
BTHR278
BVAL338
BILE447
BTHR448
BHEM500

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EL3 B 502
ChainResidue
BLEU91
BTRP339

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:19858213
ChainResidueDetails
ACYS410
BCYS410

219869

PDB entries from 2024-05-15

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