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6B11

TylHI in complex with native substrate 23-deoxy-5-O-mycaminosyl-tylonolide (23-DMTL)

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
A0016999biological_processantibiotic metabolic process
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016999biological_processantibiotic metabolic process
B0017000biological_processantibiotic biosynthetic process
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue HEM A 501
ChainResidue
ALEU110
AARG311
AALA361
APHE362
AGLY363
AHIS367
ACYS369
AGLY371
AALA375
ACGM502
AEDO512
ALEU111
AHOH643
AHOH647
AHIS118
AARG122
APHE129
AILE174
AGLY260
ATHR263
ATHR264

site_idAC2
Number of Residues17
Detailsbinding site for residue CGM A 502
ChainResidue
AGLY102
AGLU103
AGLU105
ALEU111
AALA195
AARG197
APRO198
AALA204
ALEU255
AALA306
AHEM501
AEDO512
AEDO513
AHOH634
AHOH643
AHOH666
AHOH689

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 503
ChainResidue
APHE43
AGLN277
AHIS278
ATYR302
AEDO516

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 504
ChainResidue
AASP76
AARG79
BTYR414
BGLU415

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 505
ChainResidue
AARG86
AGLU318

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 506
ChainResidue
APRO36
APRO198
ASER408
AHOH655

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 507
ChainResidue
AARG394
BTRP282
BPRO391
BALA392
BLEU393
BHOH604

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO A 508
ChainResidue
ATHR396
BARG283

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO A 509
ChainResidue
AGLU341
AALA342
ASER345

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 510
ChainResidue
ATHR153
AALA154
AEDO511
AHOH603

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 511
ChainResidue
AASP157
AEDO510
AHOH603
AHOH678

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO A 512
ChainResidue
AARG310
AHEM501
ACGM502
AEDO513
AHOH643

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO A 513
ChainResidue
AGLY308
ALEU309
AARG310
ACGM502
AEDO512

site_idAD5
Number of Residues6
Detailsbinding site for residue EDO A 514
ChainResidue
AASP398
AALA400
AHOH650
BHIS278
BALA349
BPHE350

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO A 515
ChainResidue
AGLU298
AALA356
AARG357
AHIS359

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO A 516
ChainResidue
AHIS278
AALA349
APHE350
AEDO503

site_idAD8
Number of Residues21
Detailsbinding site for residue HEM B 501
ChainResidue
BARG122
BPHE129
BLEU255
BGLY260
BTHR263
BTHR264
BMET267
BALA306
BLEU309
BARG311
BALA361
BPHE362
BGLY363
BHIS367
BCYS369
BALA375
BCGM502
BEDO504
BLEU110
BLEU111
BHIS118

site_idAD9
Number of Residues18
Detailsbinding site for residue CGM B 502
ChainResidue
BSER100
BGLY102
BGLU103
BGLU105
BLEU111
BALA195
BARG197
BPRO198
BALA204
BLEU205
BVAL254
BLEU255
BALA306
BALA409
BHEM501
BEDO504
BHOH640
BHOH653

site_idAE1
Number of Residues7
Detailsbinding site for residue EDO B 503
ChainResidue
AASP398
BHIS278
BTHR280
BALA281
BPHE350
BASP351
BILE352

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO B 504
ChainResidue
BARG310
BARG311
BHEM501
BCGM502

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO B 505
ChainResidue
AGLU56
BASP150
BASP151

site_idAE4
Number of Residues6
Detailsbinding site for residue EDO B 506
ChainResidue
BGLU262
BSER266
BLYS405
BVAL413
BHOH629
BHOH632

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGPHQCLG
ChainResidueDetails
APHE362-GLY371

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P18326
ChainResidueDetails
AHIS118
AARG122
AARG311
AHIS367
BHIS118
BARG122
BARG311
BHIS367

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P18326
ChainResidueDetails
ACYS369
BCYS369

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PDB entries from 2024-11-06

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