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3ZPI

PikC D50N mutant in P21 space group

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
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
B0016491molecular_functionoxidoreductase activity
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 Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 1408
ChainResidue
BASP222
BHOH2294
BHOH2296

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TLA A 1419
ChainResidue
AHOH2468
BARG60
BARG69
BASP303
BHOH2083
APRO30
AARG34
AEDO1415
AHOH2464
AHOH2465
AHOH2466

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 1407
ChainResidue
BLYS72
BMET92
BLEU93
BHIS100
BARG104
BPHE111
BALA243
BGLY244
BTHR247
BTHR248
BLEU251
BPRO289
BALA293
BTHR294
BARG296
BALA346
BPHE347
BGLY348
BHIS352
BCYS354
BILE355
BGLY356
BALA360
BHOH2312
BHOH2385

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1409
ChainResidue
BGLY343
BHIS344
BARG361
BEDO1410

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1410
ChainResidue
BARG62
BGLY343
BHIS344
BEDO1409

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 1407
ChainResidue
ALYS72
AMET92
ALEU93
AHIS100
AARG104
APHE111
AALA243
AGLY244
ATHR247
ATHR248
ALEU251
APRO289
AALA293
ATHR294
AARG296
AALA346
APHE347
AGLY348
AHIS352
ACYS354
AILE355
AGLY356
AALA360
AHOH2365
AHOH2434

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1408
ChainResidue
AARG104
AILE351
AHOH2469
AHOH2470

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT A 1409
ChainResidue
AASP167

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1410
ChainResidue
AGLU223
AEDO1411
AHOH2343

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1411
ChainResidue
AGLU223
AASP224
AEDO1410

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 1412
ChainResidue
AARG270
AMET273

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1413
ChainResidue
APRO330
AASP336
AARG339
AHOH2420

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FMT B 1411
ChainResidue
BGLY350

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 1412
ChainResidue
BASP209
BHOH2280
BHOH2282
BHOH2405

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1414
ChainResidue
AARG122
AVAL156
AGLU159
AHOH2472

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1415
ChainResidue
APHE24
AASP27
APRO30
ATLA1419
AHOH2040
AHOH2473
AASP23

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 1416
ChainResidue
AMET145
AARG172
AASP176

site_idBC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1417
ChainResidue
ATYR29
AARG324
AHIS333
AHOH2046
AHOH2395
AHOH2474
BASP303
BGLY306
BVAL308

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 1418
ChainResidue
AGLU291
ATYR390
APRO391
AASN392
AILE395
AHOH2033
AHOH2401

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 Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19833867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24627965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2C6H","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2C7X","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CA0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CD8","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZ7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZM","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WHW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WI9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3ZK5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7D","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7S","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4BF4","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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