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2IJ5

Crystal structure of cytochrome P450 CYP121, P212121 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0009975molecular_functioncyclase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0070025molecular_functioncarbon monoxide binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0006707biological_processcholesterol catabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0009975molecular_functioncyclase activity
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
B0020037molecular_functionheme binding
B0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
B0046872molecular_functionmetal ion binding
B0070025molecular_functioncarbon monoxide binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0006707biological_processcholesterol catabolic process
C0008395molecular_functionsteroid hydroxylase activity
C0009975molecular_functioncyclase activity
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
C0020037molecular_functionheme binding
C0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
C0046872molecular_functionmetal ion binding
C0070025molecular_functioncarbon monoxide binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0006707biological_processcholesterol catabolic process
D0008395molecular_functionsteroid hydroxylase activity
D0009975molecular_functioncyclase activity
D0016491molecular_functionoxidoreductase activity
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
D0020037molecular_functionheme binding
D0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
D0046872molecular_functionmetal ion binding
D0070025molecular_functioncarbon monoxide binding
E0004497molecular_functionmonooxygenase activity
E0005506molecular_functioniron ion binding
E0005737cellular_componentcytoplasm
E0006707biological_processcholesterol catabolic process
E0008395molecular_functionsteroid hydroxylase activity
E0009975molecular_functioncyclase activity
E0016491molecular_functionoxidoreductase activity
E0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
E0020037molecular_functionheme binding
E0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
E0046872molecular_functionmetal ion binding
E0070025molecular_functioncarbon monoxide binding
F0004497molecular_functionmonooxygenase activity
F0005506molecular_functioniron ion binding
F0005737cellular_componentcytoplasm
F0006707biological_processcholesterol catabolic process
F0008395molecular_functionsteroid hydroxylase activity
F0009975molecular_functioncyclase activity
F0016491molecular_functionoxidoreductase activity
F0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
F0020037molecular_functionheme binding
F0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
F0046872molecular_functionmetal ion binding
F0070025molecular_functioncarbon monoxide binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2820
ChainResidue
ASER61
AMET62
ALYS63
AGLN342
AHIS343
AHOH3103

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2821
ChainResidue
BASN84
BGLN342
BHIS343
BSER61
BMET62
BLYS63

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 2822
ChainResidue
CARG58
CSER61
CMET62
CLYS63
CGLN342
CHIS343
CHOH2961
CHOH3171

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 2823
ChainResidue
DARG58
DSER61
DMET62
DLYS63
DHIS343
DHOH2873
DHOH3027
DHOH3065
DHOH3200

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 E 2824
ChainResidue
DARG28
EARG58
ESER61
EMET62
ELYS63
EHIS343
EHOH2873
EHOH2905
EHOH3221
EHOH3233

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 F 2825
ChainResidue
FARG58
FSER61
FMET62
FLYS63
FHIS343
FHOH2989
FHOH3001
FHOH3158

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 462
ChainResidue
AMET62
AMET86
AHIS146
APHE230
AGLY234
ASER237
ATHR238
APHE241
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AHOH2861
AHOH2886
AHOH2888
AHOH2928
AHOH2975
AHOH2991

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 462
ChainResidue
BMET62
BMET86
BHIS146
BPHE230
BGLY234
BSER237
BTHR238
BPHE241
BPHE280
BLEU284
BARG286
BALA337
BPHE338
BGLY339
BHIS343
BCYS345
BPRO346
BHOH2845
BHOH2853
BHOH2928
BHOH2955
BHOH3010
BHOH3025

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM C 462
ChainResidue
CTHR238
CPHE241
CPHE280
CLEU284
CARG286
CALA337
CPHE338
CGLY339
CHIS343
CCYS345
CPRO346
CHOH2828
CHOH2840
CHOH2882
CHOH2916
CHOH2919
CHOH3015
CMET62
CMET86
CHIS146
CPHE230
CGLY234
CSER237

site_idBC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM D 462
ChainResidue
DMET62
DMET86
DHIS146
DALA233
DGLY234
DSER237
DPHE241
DPHE280
DLEU284
DARG286
DALA337
DPHE338
DGLY339
DHIS343
DCYS345
DPRO346
DGLY347
DHOH2837
DHOH2851
DHOH2863
DHOH2971
DHOH3000
DHOH3037

site_idBC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM E 462
ChainResidue
EMET62
EMET86
EHIS146
EPHE230
EGLY234
ESER237
EPHE241
EPHE280
ELEU284
EARG286
EALA337
EPHE338
EGLY339
EHIS343
ECYS345
EPRO346
EHOH2862
EHOH2881
EHOH2935
EHOH3017
EHOH3031
EHOH3265
EHOH3277

site_idBC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM F 462
ChainResidue
FMET62
FMET86
FHIS146
FPHE230
FGLY234
FSER237
FTHR238
FPHE280
FLEU284
FARG286
FALA337
FPHE338
FGLY339
FHIS343
FCYS345
FPRO346
FHOH2840
FHOH2927
FHOH2977
FHOH3039
FHOH3045
FHOH3059

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG
ChainResidueDetails
APHE338-GLY347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919
ChainResidueDetails
BLYS301
BGLN385
CTHR77
CSER237
CLYS301
CGLN385
DTHR77
DSER237
DLYS301
DGLN385
ETHR77
ESER237
ELYS301
EGLN385
FTHR77
FSER237
FLYS301
FGLN385
ATHR77
ASER237
ALYS301
AGLN385
BTHR77
BSER237

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASN85
BASN85
CASN85
DASN85
EASN85
FASN85

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594
ChainResidueDetails
AARG286
AHIS343
BARG286
BHIS343
CARG286
CHIS343
DARG286
DHIS343
EARG286
EHIS343
FARG286
FHIS343

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS345
BCYS345
CCYS345
DCYS345
ECYS345
FCYS345

site_idSWS_FT_FI5
Number of Residues12
DetailsSITE: Participates in a stacking interactions with the tyrosyl of cYY
ChainResidueDetails
DPHE168
DTRP182
EPHE168
ETRP182
FPHE168
FTRP182
APHE168
ATRP182
BPHE168
BTRP182
CPHE168
CTRP182

site_idSWS_FT_FI6
Number of Residues6
DetailsSITE: Important for the position of heme
ChainResidueDetails
APRO346
BPRO346
CPRO346
DPRO346
EPRO346
FPRO346

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PDB entries from 2024-05-15

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