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3NC5

CYP134A1 structure with an open substrate binding loop

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
A0016713molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
A0020037molecular_functionheme binding
A0046148biological_processpigment biosynthetic process
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016713molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
B0020037molecular_functionheme binding
B0046148biological_processpigment biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 406
ChainResidue
ALEU64
AHIS351
ACYS353
AGLY355
APHE358
AGOL407
AHOH427
AASN229
AALA233
AALA234
APRO237
ATHR241
AARG285
AALA345
APHE346

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
APRO237
AVAL280
ATYR391
AHEM406
AHOH427

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 408
ChainResidue
AASP163
ATHR166
ASER167

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 409
ChainResidue
AGLN281
AMET307
AILE308
AGLY309

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 406
ChainResidue
BGLU66
BILE97
BASN229
BALA233
BALA234
BPRO237
BLEU274
BILE283
BARG285
BALA345
BPHE346
BHIS351
BCYS353
BGLU362
BILE363
BHOH422

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 407
ChainResidue
BALA233
BPRO237
BTYR391
BHOH422

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 408
ChainResidue
BILE97
BVAL354
BGLY355
BTHR356
BALA357
BPHE358

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGIHNCVG
ChainResidueDetails
APHE346-GLY355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20690619
ChainResidueDetails
AARG285
BLYS62
BASN229
BARG285
ALYS62
AASN229

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS353
BCYS353

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PDB entries from 2024-06-12

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