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3CXX

Crystal structure of cytochrome P450 CYP121 F338H from M. 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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 819
ChainResidue
AHOH1059
AHOH1250
ASER12
AARG14
AHOH1048

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 820
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH897
AHOH933

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HEM A 462
ChainResidue
AMET62
AMET86
AHIS146
APHE230
AGLY234
ASER237
ATHR238
APHE241
ALEU274
APHE280
ALEU284
AARG286
AALA337
AHIS338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
ALEU350
AGLY351
AHOH894
AHOH940
AHOH945
AHOH967
AHOH972
AHOH1006
AHOH1071

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

237423

PDB entries from 2025-06-11

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