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5IBI

Crystal structure Mycobacterium tuberculosis CYP121 in complex with inhibitor fragment 26a

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 Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH602

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH521
AHOH531
AHOH582
AHOH644
AHOH690
AHOH773
ASER12
AARG14

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH513
AHOH529

site_idAC4
Number of Residues15
Detailsbinding site for residue 69U A 404
ChainResidue
ATHR65
AARG72
ALEU76
ATHR77
AVAL78
AASN85
AALA167
APHE168
ATRP182
AVAL228
AGLN385
AHEM405
AHOH525
AHOH657
AHOH696

site_idAC5
Number of Residues21
Detailsbinding site for residue HEM A 405
ChainResidue
AMET62
AMET86
AHIS146
AGLY234
ASER237
APHE241
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
A69U404
AHOH512
AHOH574
AHOH630
AHOH637
AHOH657
AHOH685

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
ASER237
ALYS301
AGLN385
ATHR77

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
ATRP182
APHE168

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

218500

PDB entries from 2024-04-17

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