Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4B7D

PikC bound to the 10-DML analog with the 3-(N,N-dimethylamino) propanoate anchoring 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
A0033068biological_processmacrolide biosynthetic process
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
B0033068biological_processmacrolide biosynthetic process
B0046872molecular_functionmetal ion binding
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1406
ChainResidue
ATRP74
ATHR294
ATYR295
AQLE1408
AHOH2075
AHOH2226

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 1407
ChainResidue
AHIS100
AARG104
APHE111
ALEU240
AALA243
AGLY244
ATHR247
ATHR248
ALEU251
APRO289
AALA293
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
AHIS352
ACYS354
AILE355
AGLY356
AALA360
AQLE1408
AHOH2212
ALYS72
AMET92
ALEU93

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE QLE A 1408
ChainResidue
AGLU85
ALEU93
AGLU94
AHIS238
AILE239
AVAL242
AALA243
AMET394
AGOL1406
AHEM1407

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1406
ChainResidue
BTHR294
BTYR295
BMET394
BQLE1408
BHOH2068

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM B 1407
ChainResidue
BLYS72
BMET92
BLEU93
BHIS100
BARG104
BILE157
BILE239
BLEU240
BALA243
BGLY244
BTHR247
BTHR248
BLEU251
BPRO289
BALA293
BTHR294
BARG296
BALA346
BPHE347
BILE351
BHIS352
BCYS354
BILE355
BALA360
BQLE1408
BHOH2204

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE QLE B 1408
ChainResidue
BTRP74
BGLU85
BLEU93
BGLU94
BHIS238
BVAL242
BALA243
BTHR247
BMET394
BILE395
BGOL1406
BHEM1407

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 1409
ChainResidue
BASP182
BTHR341
BALA342
BGLY343
BHIS344
BPHE353
BARG361
BHOH2170
BHOH2202
BHOH2220

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG
ChainResidueDetails
APHE347-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459
ChainResidueDetails
AGLU94
AALA187
AHIS238
BGLU94
BALA187
BHIS238

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H, ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0, ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S, ECO:0000312|PDB:4BF4
ChainResidueDetails
ACYS354
BCYS354

223790

PDB entries from 2024-08-14

PDB statisticsPDBj update infoContact PDBjnumon