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4DNZ

The crystal structures of CYP199A4

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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AILE97
AARG300
AGLY350
APHE351
AGLY352
AHIS356
ACYS358
AGLY360
AHOH632
ALEU98
AHIS105
AARG109
AALA248
AGLY249
ATHR252
ATHR253
APHE298

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG109
AGOL503
AHOH676
DLYS114

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ASER113
AVAL359
AGLN361
ASO4502

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
ATYR177
AGLN203

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 501
ChainResidue
BILE97
BLEU98
BHIS105
BARG109
BPHE160
BALA248
BGLY249
BTHR252
BTHR253
BPHE298
BARG300
BGLY350
BPHE351
BGLY352
BHIS356
BCYS358
BGLY360
BHOH671
BHOH704

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BARG109
BGOL503
BHOH611
CLYS114

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
BSER113
BLEU116
BSER117
BGLN361
BLEU362
BSO4502

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BTYR177
BGLN203

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM C 501
ChainResidue
CILE97
CLEU98
CHIS105
CARG109
CPHE160
CALA248
CGLY249
CTHR252
CTHR253
CVAL295
CPHE298
CARG300
CGLY350
CPHE351
CGLY352
CHIS356
CCYS358
CVAL359
CGLY360
CHOH648

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 502
ChainResidue
BLYS114
CARG109
CSER113
CGOL503

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 503
ChainResidue
CSER113
CLEU116
CSER117
CGLN361
CLEU362
CSO4502

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 504
ChainResidue
CARG92
CTYR177
CGLN203
CARG243

site_idBC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM D 501
ChainResidue
DGLY249
DTHR252
DTHR253
DVAL295
DPHE298
DARG300
DGLY350
DPHE351
DVAL355
DHIS356
DCYS358
DVAL359
DGLY360
DALA364
DHOH613
DLEU68
DILE97
DLEU98
DHIS105
DARG109
DLEU245
DALA248

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 502
ChainResidue
ALYS114
DARG109
DSER113
DGOL503

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 503
ChainResidue
DSER113
DLEU116
DSER117
DVAL359
DGLN361
DSO4502

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL D 504
ChainResidue
DTYR177
DGLN203

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGVHMCVG
ChainResidueDetails
APHE351-GLY360

223790

PDB entries from 2024-08-14

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