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4IQ7

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 Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
A1G9406
AHOH501
AHOH524
AMET86
AHOH613
AHOH667
AHOH1068
AHIS146
AGLY234
ASER237
ATHR238
APHE241
APHE280
ALEU284

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH796
AHOH841
AHOH1087

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ASER12
AARG17
AHOH673
AHOH713
AHOH769
AHOH900

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AVAL5
ALEU7
AARG32
AARG300
AHOH786

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AARG134
AASN135
APHE161
AARG381
AARG391
AHOH563
AHOH575

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1G9 A 406
ChainResidue
AMET62
AVAL78
AVAL83
AASN85
AALA167
APHE168
ATHR229
AALA233
AARG386
AHEM401
AHOH540
AHOH546
AHOH752
AHOH874

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
AALA3
ATHR4
AVAL5
ALYS301

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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