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5EX6

Structure of P450 StaH from glycopeptide antibiotic A47934 biosynthesis

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
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO C 501
ChainResidue
CASN240
CALA285
CHEM502
CHOH607
CHOH615

site_idAC2
Number of Residues23
Detailsbinding site for residue HEM C 502
ChainResidue
CLEU152
CMET233
CALA236
CGLY237
CASN240
CPRO283
CPRO286
CTHR287
CARG289
CLEU312
CALA339
CPHE340
CGLY341
CVAL344
CHIS345
CCYS347
CEDO501
CHOH607
CHOH629
CLEU88
CMET89
CHIS96
CARG100

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 501
ChainResidue
ALEU235
AALA236
AGLY237
AASP238
AASP239
AASN240
AEDO502

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 502
ChainResidue
AMET89
AASN240
AALA285
AGOL501
AHOH615

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 503
ChainResidue
AASN87
ALEU88
AMET89
AGLN232

site_idAC6
Number of Residues21
Detailsbinding site for residue HEM A 504
ChainResidue
ALEU88
AMET89
AHIS96
AARG100
ALEU155
AMET233
AALA236
AGLY237
AASN240
AMET244
APRO286
ATHR287
AARG289
AALA339
APHE340
AGLY341
AHIS345
ACYS347
AGLY349
AHOH615
AHOH641

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL B 501
ChainResidue
AARG60
AGLU293
BLEU169
BARG172
BALA186
BALA189

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL B 502
ChainResidue
BLEU235
BALA236
BASN240
BHEM503
BHOH601

site_idAC9
Number of Residues22
Detailsbinding site for residue HEM B 503
ChainResidue
BLEU88
BMET89
BHIS96
BARG100
BLEU152
BALA236
BGLY237
BASN240
BPRO283
BPRO286
BTHR287
BARG289
BALA339
BPHE340
BGLY341
BVAL344
BHIS345
BCYS347
BGLY349
BGOL502
BHOH601
BHOH632

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGVHHCLG
ChainResidueDetails
CPHE340-GLY349

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PDB entries from 2025-07-09

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