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4FMX

Crystal Structure of Substrate-Bound P450cin

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
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0020037molecular_functionheme binding
A0046232biological_processcarbazole catabolic 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
B0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
B0020037molecular_functionheme binding
B0046232biological_processcarbazole catabolic process
B0046872molecular_functionmetal ion binding
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AASN73
AASN242
ATHR243
AARG289
APHE312
ASER339
ALEU340
AGLY341
AILE344
AHIS345
ACYS347
AVAL76
AILE353
ACNL502
AHOH630
AHOH959
AMET90
AALA91
AHIS98
AARG102
APHE109
AILE234
AGLY238

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CNL A 502
ChainResidue
AASN242
AVAL386
AHEM501

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG346
AALA350
AHIS351
AARG354
AHOH821

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
AARG253
AASP257
AGLU259
AARG263
AILE328
AGOL505
AHOH615
AHOH649
BARG253

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
AARG253
AASN327
AGOL504
BARG253
BASP257
BGLU259
BARG263
BILE328
BHOH619
BHOH630

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM B 501
ChainResidue
BASN73
BVAL76
BMET90
BALA91
BHIS98
BARG102
BILE234
BGLY238
BASN242
BTHR243
BARG289
BPHE312
BSER339
BLEU340
BGLY341
BILE344
BHIS345
BCYS347
BLEU348
BILE353
BCNL502
BHOH663

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CNL B 502
ChainResidue
BASN242
BVAL287
BHEM501

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BARG346
BALA350
BHIS351
BARG354
BHOH806

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 504
ChainResidue
BPRO272
BARG354
BARG358
BHOH918
BHOH950
BHOH956
BHOH988

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15260491, ECO:0000269|PubMed:18270198, ECO:0000269|PubMed:22775403
ChainResidueDetails
AASN73
BHIS345
AHIS98
AARG102
AARG289
AHIS345
BASN73
BHIS98
BARG102
BARG289

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15260491
ChainResidueDetails
AASN242
BASN242

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS347
BCYS347

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Controls regioselective substrate oxidation
ChainResidueDetails
AASN242
BASN242

226707

PDB entries from 2024-10-30

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