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2Y5N

Structure of the mixed-function P450 MycG in complex with mycinamicin V in P21 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
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
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0017000biological_processantibiotic biosynthetic process
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 450
ChainResidue
ALEU83
AGLN242
APHE286
AARG288
AGLY338
APHE339
AGLY340
AHIS344
ACYS346
ALEU347
AGLY348
ALEU84
AALA352
AMYV460
AHOH2397
AHOH2566
AHOH2567
AHIS91
AARG95
APHE102
AALA234
AGLY235
ASER238
ATHR239

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MYV A 460
ChainResidue
AARG75
AVAL79
AGLY81
AGLY82
ALEU84
APHE168
AVAL174
AMET179
AVAL233
AALA234
ALEU386
AHEM450
AHOH2313
AHOH2399
AHOH2569
AHOH2570
AHOH2571

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1398
ChainResidue
AARG113
AGLU120
AARG145
ASER155
AHIS158
AHOH2572

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1399
ChainResidue
ATHR18
ALEU19
AALA20
AGLY21
AHOH2573

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1400
ChainResidue
AGLU292
AHOH2575
AHOH2576

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1401
ChainResidue
AGLY191
AASP195
AHOH2346
AHOH2578

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1402
ChainResidue
AARG140
ATHR240
ATHR241
AALA244
AGLY389
APRO390
ALEU391
AHOH2579

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1403
ChainResidue
AARG140
ATHR171
ALEU391
AHOH2311
AHOH2561
AHOH2581
AHOH2582

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1404
ChainResidue
AASP325
AHOH2483
AHOH2485

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1405
ChainResidue
AARG73
ATHR74
AVAL282
AGLY283
AALA285
AMET385
ALEU386
AHOH2439
AHOH2583
AHOH2584

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1406
ChainResidue
AHOH2103
AHOH2251
AHOH2260
AHOH2263

site_idBC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 450
ChainResidue
BTHR239
BALA285
BPHE286
BARG288
BGLY338
BPHE339
BGLY340
BHIS344
BCYS346
BGLY348
BMYV460
BHOH2381
BHOH2543
BLEU83
BLEU84
BHIS91
BARG95
BPHE102
BALA234
BGLY235
BSER238

site_idBC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MYV B 460
ChainResidue
BARG75
BGLU77
BVAL79
BGLY81
BGLY82
BLEU83
BLEU84
BPHE168
BSER170
BVAL174
BMET179
BVAL233
BALA234
BLEU386
BHEM450
BHOH2545
BHOH2546
BHOH2547

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1398
ChainResidue
BARG253
BGLU255
BILE327
BHOH2464
BHOH2469

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1399
ChainResidue
BARG140
BTHR240
BTHR241
BALA244
BGLY389
BPRO390
BLEU391
BHOH2548

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1400
ChainResidue
BLEU56
BGLY57
BGLY59
BPHE61
BPRO88
BGLY342
BVAL343
BHOH2201
BHOH2549

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1401
ChainResidue
BTHR2
BARG34
BGLU41
BGLU42
BALA43
BTRP44
BGLU305
BPRO306
BHOH2551

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1402
ChainResidue
BTYR248
BTHR252
BARG253
BGLU376
BHOH2552
BHOH2553

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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22952225, ECO:0007744|PDB:2Y46, ECO:0007744|PDB:2Y98, ECO:0007744|PDB:3ZSN
ChainResidueDetails
AGLY81
BGLY81

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22952225
ChainResidueDetails
AHIS91
AARG95
AARG288
AHIS344
BHIS91
BARG95
BARG288
BHIS344

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:22952225, ECO:0007744|PDB:2Y5N, ECO:0007744|PDB:2Y98, ECO:0007744|PDB:2YCA
ChainResidueDetails
ACYS346
BCYS346

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PDB entries from 2024-07-10

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