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2Y98

Structure of the mixed-function P450 MycG in complex with mycinamicin IV in P21212 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 450
ChainResidue
ALEU83
ASER238
ATHR239
AGLN242
AALA285
APHE286
AARG288
AGLY338
APHE339
AGLY340
AHIS344
ALEU84
ACYS346
AGLY348
AALA352
AMIV460
AHOH2248
AHOH2388
AHIS91
AARG95
APHE102
AILE147
ALEU231
AALA234
AGLY235

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MIV A 460
ChainResidue
AARG75
AGLU77
AVAL79
AGLY81
AGLY82
ALEU84
APHE168
ASER170
AVAL174
AVAL233
AALA234
ALEU386
AHEM450
AHOH2206
AHOH2389
AHOH2390

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1398
ChainResidue
AARG145
AHIS158
AHOH2156

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1399
ChainResidue
AARG48
ALYS100
AARG297
AHOH2391

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1400
ChainResidue
AALA20
AGLY21
AARG22
AARG53
AGLN335
AHIS341
AHOH2065
AHOH2393
AHOH2394
AHOH2395

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1401
ChainResidue
ALEU56
AGLY57
AGLY59
APRO88
AASP325
AGLY342
AVAL343
AHOH2116
AHOH2320
AHOH2396

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1402
ChainResidue
AARG140
ATHR240
AALA244
AGLY389
APRO390
ALEU391
AHOH2397

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHHCLG
ChainResidueDetails
APHE339-GLY348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y46","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZSN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22952225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y5N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YCA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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