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4IPS

Substrate and reaction specificity of Mycobacterium tuberculosis cytochrome P450 CYP121

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
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
A0046872molecular_functionmetal ion binding
A0070025molecular_functioncarbon monoxide binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
ASO4403
A1G4404
AHOH563
AMET86
AHOH696
AHOH724
AHOH745
AHOH1043
AHOH1091
AHIS146
APHE230
AGLY234
ASER237
APHE241
APHE280
ALEU284

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AASN84
AHIS343
AHOH782
AHOH846
AHOH1003
AHOH1087

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AALA233
AARG386
AHEM401
A1G4404
AHOH521
AHOH724

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1G4 A 404
ChainResidue
AMET62
AVAL78
AVAL82
AVAL83
AASN85
AALA167
ATHR229
APRO285
AHEM401
ASO4403
AHOH548
AHOH633
AHOH699
AHOH712
AHOH1015

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AASP16
ASER248
AGLN251
AARG252
AILE276
AHOH544
AHOH1017
AHOH1027

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
AVAL5
AGLU8
AALA68
AGLY69
AALA70
APRO71
AGLY302

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
AVAL5
AGLU64
ALEU287
AALA288
ATHR289
ALYS301
AGLY302
AHOH822
AHOH1090

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 408
ChainResidue
AARG59
AASP291
AILE292
AGLN293
AHOH1034

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
ALEU193
AILE198
ASER207
ALYS211
AARG340
AHOH587
AHOH602
AHOH634
AHOH672
AHOH779

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 410
ChainResidue
AHOH569
AHOH630
AARG134
APHE161
AARG381
AARG391
AHOH555

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919
ChainResidueDetails
ATHR77
ASER237
ALYS301
AGLN385

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASN85

site_idSWS_FT_FI3
Number of Residues2
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

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS345

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Participates in a stacking interactions with the tyrosyl of cYY
ChainResidueDetails
APHE168
ATRP182

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for the position of heme
ChainResidueDetails
APRO346

237735

PDB entries from 2025-06-18

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