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5KYO

Crystal Structure of CYP101J2

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
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
E0004497molecular_functionmonooxygenase activity
E0005506molecular_functioniron ion binding
E0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
F0004497molecular_functionmonooxygenase activity
F0005506molecular_functioniron ion binding
F0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue HEM A 501
ChainResidue
AASN84
ASER299
AARG301
ATHR351
APHE352
AHIS357
ACYS359
APRO360
AGLY361
ALEU364
AALA365
ALEU103
AHOH643
AHOH647
AHOH710
AHOH759
AHOH814
AHIS110
AVAL247
AGLY250
AGLY251
ATHR254
APHE291
AVAL297

site_idAC2
Number of Residues26
Detailsbinding site for residue HEM B 501
ChainResidue
BASN84
BLEU103
BHIS110
BVAL247
BGLY250
BGLY251
BTHR254
BMET258
BPHE291
BVAL297
BSER299
BARG301
BTHR351
BPHE352
BGLY353
BHIS357
BCYS359
BPRO360
BGLY361
BLEU364
BALA365
BHOH671
BHOH688
BHOH752
BHOH760
BHOH801

site_idAC3
Number of Residues22
Detailsbinding site for residue HEM C 501
ChainResidue
CASN84
CLEU103
CHIS110
CLEU121
CVAL247
CGLY250
CGLY251
CTHR254
CVAL255
CVAL297
CSER299
CARG301
CTHR351
CHIS357
CCYS359
CPRO360
CGLY361
CALA365
CHOH644
CHOH659
CHOH695
CHOH734

site_idAC4
Number of Residues21
Detailsbinding site for residue HEM D 501
ChainResidue
DASN84
DLEU103
DHIS110
DLEU117
DVAL247
DGLY250
DGLY251
DTHR254
DMET258
DSER299
DARG301
DTHR351
DPHE352
DGLY353
DHIS357
DCYS359
DPRO360
DLEU364
DHOH641
DHOH659
DHOH677

site_idAC5
Number of Residues24
Detailsbinding site for residue HEM E 501
ChainResidue
ETHR254
EMET258
EPHE291
ESER299
EARG301
ETHR351
EPHE352
EGLY353
EHIS357
ECYS359
EPRO360
EGLY361
ELEU364
EALA365
EHOH629
EHOH680
EHOH687
EHOH709
EASN84
ELEU103
EHIS110
EVAL247
EGLY250
EGLY251

site_idAC6
Number of Residues23
Detailsbinding site for residue HEM F 501
ChainResidue
FASN84
FLEU103
FHIS110
FVAL247
FGLY250
FGLY251
FTHR254
FVAL255
FVAL297
FSER299
FARG301
FTHR351
FPHE352
FGLY353
FHIS357
FCYS359
FPRO360
FGLY361
FALA365
FHOH615
FHOH629
FHOH672
FHOH714

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGkGSHTCPG
ChainResidueDetails
APHE352-GLY361

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PDB entries from 2024-10-09

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