Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3R9B

Crystal structure of Mycobacterium smegmatis CYP164A2 in ligand free state

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
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APHE97
ALEU264
AMET297
AVAL303
AARG308
AGLY358
APHE359
AGLY360
AALA363
AHIS364
ACYS366
ALEU98
AGLY368
AALA372
AD12509
AHOH615
AHOH696
AHIS105
AARG109
AILE159
ALEU252
ALEU253
AALA256
ATHR260

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AGLU235
ATHR242
AGLU243
AK507
AHOH707
AHOH828

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
AARG109
ASER113
ANA506
AHOH744
AHOH834
BASN50
BARG81

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AVAL341
AGLY342
AARG351
AGLN353

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AILE78
ATYR309
ATHR326
AHOH753
AHOH775

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 506
ChainResidue
AGLY110
ASER113
APO4503
AHOH835

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 507
ChainResidue
AGLU235
AGLY238
ALEU241
APO4502
AHOH785

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
AARG109
AGLY362
AALA363
AHOH835
BPRO47
BGLU48
BARG81

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE D12 A 509
ChainResidue
ALEU252
AALA256
AHEM501

site_idBC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 501
ChainResidue
BPHE97
BLEU98
BHIS105
BARG109
BILE159
BLEU252
BLEU253
BALA256
BTHR260
BTHR261
BLEU264
BMET297
BVAL303
BARG308
BGLY358
BPHE359
BGLY360
BALA363
BHIS364
BCYS366
BGLY368
BALA372
BD12509
BHOH668
BHOH669

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BGLU235
BTHR242
BGLU243
BK508
BHOH741

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
BEDO506
BVAL341
BGLY342
BARG351
BGLN353

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
BSER76
BILE78
BTYR309
BTHR326
BHOH646
BHOH822

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 505
ChainResidue
BALA343
BARG346
CASP350
CARG351
CALA352

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
BGLY342
BARG346
BASP348
BARG351
BEDO503

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 507
ChainResidue
BSER56
BASP59
BGLY317
BHOH647

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 508
ChainResidue
BGLU235
BGLY238
BLEU241
BPO4502

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D12 B 509
ChainResidue
BLEU98
BLEU184
BASN251
BHEM501

site_idCC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM C 501
ChainResidue
CPHE97
CLEU98
CHIS105
CARG109
CILE159
CLEU252
CLEU253
CALA256
CTHR260
CTHR261
CLEU264
CMET297
CVAL303
CARG308
CGLY358
CPHE359
CGLY360
CHIS364
CCYS366
CGLY368
CALA372
CD12513
CHOH642
CHOH654

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 502
ChainResidue
CGLU235
CTHR242
CGLU243
CK512
CHOH687

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 503
ChainResidue
BARG109
BSER113
CASN50
CARG81
CNA511
CHOH614
CHOH772

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO C 504
ChainResidue
CALA183
CASP185
CPHE187
CLEU188
CHOH627
CHOH656
CHOH727
CHOH757

site_idCC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO C 505
ChainResidue
APRO47
AGLU48
AARG81
CARG109
CGLY362
CALA363
CEDO508
CHOH779

site_idCC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 506
ChainResidue
CVAL341
CGLY342
CARG351
CGLN353

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 507
ChainResidue
BARG109
BALA363
BHOH602
CPRO47
CGLU48
CARG81

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 508
ChainResidue
CARG109
CGLY110
CSER113
CEDO505
CHOH779
CHOH819

site_idCC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 509
ChainResidue
CSER76
CPHE79
CTYR309
CTHR326
CHOH727
CHOH790

site_idDC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 510
ChainResidue
CSER56
CASP59
CGLY317
CHOH641

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 511
ChainResidue
BGLY110
BSER113
BHOH602
CPO4503
CHOH825

site_idDC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 512
ChainResidue
CGLU235
CGLY238
CLEU241
CPO4502
CHOH648

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE D12 C 513
ChainResidue
CLEU184
CLEU252
CILE255
CALA256
CHEM501

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGkGAHFCLG
ChainResidueDetails
APHE359-GLY368

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon