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6RQB

CYP121 in complex with 3-bromo dicyclotyrosine

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 Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH502

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH757
AHOH779
ASER12
AHOH670

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH501
AHOH547

site_idAC4
Number of Residues17
Detailsbinding site for residue Q47 A 404
ChainResidue
AMET62
ATHR77
AVAL78
AVAL82
AVAL83
AASN85
AALA167
APHE168
ATHR229
AARG386
AHEM405
ASO4406
AHOH504
AHOH525
AHOH545
AHOH590
AHOH605

site_idAC5
Number of Residues21
Detailsbinding site for residue HEM A 405
ChainResidue
AMET62
AMET86
AHIS146
AGLY234
ASER237
ATHR238
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AQ47404
AHOH518
AHOH519
AHOH545
AHOH560
AHOH745

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 406
ChainResidue
AASN74
AGLN385
AQ47404
AHOH608
AHOH618

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

239803

PDB entries from 2025-08-06

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