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6H1L

Structure of the BM3 heme domain in complex with tioconazole

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
A0020037molecular_functionheme binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue FJQ A 501
ChainResidue
AALA74
ALEU437
AHEM502
AEDO509
AHOH703
ALEU75
AVAL78
APHE82
AVAL87
ATHR260
AILE263
AALA264
ATHR268

site_idAC2
Number of Residues25
Detailsbinding site for residue HEM A 502
ChainResidue
ALYS69
ALEU86
AVAL87
ATRP96
APHE107
AALA264
ATHR268
ATHR327
AALA328
APHE331
APRO392
APHE393
AGLY394
AARG398
AALA399
ACYS400
AILE401
AGLY402
AFJQ501
AHOH622
AHOH689
AHOH694
AHOH696
AHOH698
AHOH706

site_idAC3
Number of Residues2
Detailsbinding site for residue PO4 A 503
ChainResidue
AGLU137
AHIS138

site_idAC4
Number of Residues5
Detailsbinding site for residue PO4 A 504
ChainResidue
ALYS364
ATHR365
AILE366
ATRP367
AGLY368

site_idAC5
Number of Residues6
Detailsbinding site for residue TLA A 505
ChainResidue
ALEU29
ATYR51
AALA74
AEDO507
AEDO508
AEDO509

site_idAC6
Number of Residues5
Detailsbinding site for residue DIO A 506
ChainResidue
AILE366
ATRP367
AARG378
AALA384
AHOH758

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 507
ChainResidue
AMET185
ATLA505

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO A 508
ChainResidue
APRO329
ATHR436
ALEU437
ATHR438
ALEU439
ATLA505
AEDO509
AHOH673

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO A 509
ChainResidue
AALA328
APRO329
AALA330
AFJQ501
ATLA505
AEDO508

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 510
ChainResidue
ATYR166
AARG167
AHOH608
AHOH780

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO A 511
ChainResidue
ATRP90
AHIS92
ATYR334
AHOH776
BPRO18
BASN21

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO A 512
ChainResidue
AHIS236
AGLY240
ALYS241

site_idAD4
Number of Residues11
Detailsbinding site for residue FJQ B 501
ChainResidue
BALA74
BLEU75
BVAL78
BPHE82
BVAL87
BTHR260
BILE263
BALA264
BTHR268
BLEU437
BHEM502

site_idAD5
Number of Residues24
Detailsbinding site for residue HEM B 502
ChainResidue
BTRP96
BPHE261
BALA264
BGLY265
BTHR268
BTHR269
BPHE331
BPRO392
BPHE393
BGLY394
BARG398
BALA399
BCYS400
BILE401
BGLY402
BFJQ501
BHOH609
BHOH622
BHOH663
BHOH712
BHOH772
BLYS69
BLEU86
BVAL87

site_idAD6
Number of Residues4
Detailsbinding site for residue PO4 B 503
ChainResidue
BGLU137
BHIS138
BHOH683
BHOH776

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO B 504
ChainResidue
BARG378
BILE385

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO B 505
ChainResidue
BLEU311
BGLY315
BTHR411

site_idAD9
Number of Residues6
Detailsbinding site for residue EDO B 506
ChainResidue
BTRP130
BGLU131
BLEU133
BALA448
BLYS449
BSER450

site_idAE1
Number of Residues5
Detailsbinding site for residue EDO B 507
ChainResidue
BVAL281
BLEU287
BPHE423
BGLU424
BASP425

site_idAE2
Number of Residues4
Detailsbinding site for residue PEG B 508
ChainResidue
BPHE81
BILE209
BMET212
BASN213

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG
ChainResidueDetails
APHE393-GLY402

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PDB entries from 2024-07-17

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