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4IPW

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
A1G7406
AHOH501
AHOH524
AMET86
AHOH567
AHOH613
AHOH722
AHOH1088
AHIS146
APHE230
AGLY234
ASER237
APHE241
APHE280
ALEU284

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH784
AHOH793
AHOH834
AHOH1082
AHOH1107

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ASER12
AARG17
AHOH672
AHOH711
AHOH766
AHOH890

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ALEU7
AARG32
AARG300
AHOH783

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AARG134
AASN135
APHE161
AARG381
AARG391
AHOH563
AHOH657

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 1G7 A 406
ChainResidue
AMET62
ATHR77
AVAL78
AVAL82
AVAL83
AASN85
AALA167
APHE168
ATHR229
AARG386
AHEM401
AHOH502
AHOH540
AHOH546
AHOH567
AHOH623
AHOH751
AHOH865

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
AMET62
ATHR65
AARG72
AASN74
ALEU76
APRO285
AHOH566
AHOH751
AHOH972

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 408
ChainResidue
AVAL5
AGLU64
AALA67
ATHR289
ALYS301
AHOH868
AHOH889
AHOH1026

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AVAL5
AGLU8
AALA68
AGLY69
AALA70
APRO71
AGLY302
AHOH1026

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 410
ChainResidue
AHOH760
AHOH761
AHOH902
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 411
ChainResidue
AGLU81
ATRP182
AILE186
AGLU221
ATHR225
AGLN254
AHOH573
AHOH625
AHOH626
AHOH875

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 412
ChainResidue
AASP16
ASER248
AGLN251
AARG252
AILE276
AHOH560
AHOH764
AHOH1132

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

219140

PDB entries from 2024-05-01

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