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5FOI

Crystal structure of mycinamicin VIII C21 methyl hydroxylase MycCI from Micromonospora griseorubida bound to mycinamicin VIII

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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 413
ChainResidue
AMET79
AALA274
ALEU277
AARG279
ALEU302
AALA329
APHE330
AGLY331
AHIS335
ACYS337
AGLY339
ALEU80
AGOL1389
AHOH2071
AHIS87
AARG91
ALEU224
AGLY228
ATHR231
ASER232
ALEU268

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MY8 A 414
ChainResidue
AALA69
AGLY71
APHE76
ALEU80
AMET81
AALA164
APRO167
ASER172
AMET173
ALEU223
AGOL1389
AHOH2028
AHOH2076

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 413
ChainResidue
BMET79
BLEU80
BHIS87
BARG91
BPHE98
BILE143
BLEU224
BALA227
BTHR231
BLEU277
BARG279
BALA329
BPHE330
BHIS335
BCYS337
BMY8414
BHOH2065

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MY8 B 414
ChainResidue
BALA69
BGLY71
BASP72
BLEU80
BALA164
BPRO167
BSER172
BMET173
BLEU223
BHEM413

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1389
ChainResidue
ALEU277
AARG278
APRO377
AHEM413
AMY8414
AHOH2029
AHOH2062

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1390
ChainResidue
AGLN256
APRO257
AGLU258
BARG91
BILE95
BHOH2022

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SPD A 1391
ChainResidue
AASP153
APHE156
AGLU178
AGLU181
ASPD1392
ASPD1393

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SPD A 1393
ChainResidue
ASPD1391

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SPD A 1392
ChainResidue
APHE156
AGLU181
ASPD1391
BGLU178

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGPHQCLG
ChainResidueDetails
APHE330-GLY339

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P18326
ChainResidueDetails
AHIS87
AARG91
AARG279
AHIS335
BHIS87
BARG91
BARG279
BHIS335

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P18326
ChainResidueDetails
ACYS337
BCYS337

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PDB entries from 2024-11-13

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