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6GEO

Crystal structure of Mycobacterium tuberculosis cytochrome P450 CYP121A1 in complex with Triazole Pyrazole inhibitor 10j

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 Residues24
Detailsbinding site for residue HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
ASO4402
AEW2405
AHOH525
AMET86
AHOH575
AHOH579
AHOH613
AHOH712
AHOH860
AHIS146
APHE230
AGLY234
ASER237
APHE241
APHE280
ALEU284

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AARG386
AHEM401
AHOH525
AHOH586

site_idAC3
Number of Residues10
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH527
AHOH563
AHOH581
AHOH711
AHOH751

site_idAC4
Number of Residues11
Detailsbinding site for residue SO4 A 404
ChainResidue
ASER219
AARG252
ASER324
AILE325
AHOH508
AHOH521
AHOH531
AHOH706
AHOH778
AHOH835
AHOH841

site_idAC5
Number of Residues12
Detailsbinding site for residue EW2 A 405
ChainResidue
ALEU76
ATHR77
AVAL78
AVAL82
AASN85
AALA167
APHE168
AVAL228
AGLN385
AHEM401
AHOH625
AHOH724

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

224931

PDB entries from 2024-09-11

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