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1N40

Atomic structure of CYP121, a mycobacterial P450

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 Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 817
ChainResidue
ALYS211
AHOH1334
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH967
AHOH990
AHOH1079

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 819
ChainResidue
ASER12
AHOH1015
AHOH1125
AHOH1196
AHOH1370

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 820
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH907
AHOH931
AHOH1037
AHOH1476
AHOH1518

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HEM A 462
ChainResidue
AMET62
AMET86
AHIS146
APHE230
AALA233
AGLY234
ASER237
ATHR238
ALEU274
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
AGLY351
AOXY501
AHOH869
AHOH878
AHOH912
AHOH924
AHOH959
AHOH1059
AHOH1123

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXY A 501
ChainResidue
ASER237
APHE280
AARG386
AHEM462
AHOH912
AHOH1372

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

218853

PDB entries from 2024-04-24

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