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3CY0

Crystal structure of cytochrome P450 CYP121 S237A mutant from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
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
A0046872molecular_functionmetal ion binding
A0070025molecular_functioncarbon monoxide binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 817
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 819
ChainResidue
ASER12
AARG14

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 820
ChainResidue
ASER61
AMET62
ALYS63
AHIS343
AHOH940
AARG58

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 462
ChainResidue
AMET62
AMET86
AHIS146
APHE230
AGLY234
AALA237
ATHR238
APHE241
APHE280
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
AHOH870
AHOH892
AHOH949
AHOH951
AHOH962
AHOH1017

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 site: {"evidences":[{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12435731","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17028183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18818197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19416919","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22890978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23620594","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Participates in a stacking interactions with the tyrosyl of cYY"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Important for the position of heme"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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