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

3NC3

CYP134A1 structure with a closed 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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 406
ChainResidue
ALYS62
AARG285
AALA345
APHE346
AHIS351
ACYS353
AVAL354
AGLY355
APHE358
AALA359
AILE363
AILE97
AGOL407
AHOH428
AMET143
AASN229
AALA233
AALA234
APRO237
ATHR241
AILE283

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
AASN229
ATYR391
AHEM406
AHOH428

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 408
ChainResidue
AASN252
AGLU254
BARG342

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 409
ChainResidue
ALYS277

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 410
ChainResidue
APRO172
AARG175
BASN114

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 411
ChainResidue
AHIS248
AASN251
AASN252

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 406
ChainResidue
BSER63
BLEU64
BMET143
BASN229
BALA233
BALA234
BPRO237
BTHR241
BILE283
BARG285
BALA345
BHIS351
BCYS353
BVAL354
BGLY355
BPHE358
BALA359
BILE363
BGOL407
BHOH431

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 407
ChainResidue
BLEU64
BALA233
BVAL280
BTYR391
BTHR392
BHEM406
BHOH431
BHOH432

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 408
ChainResidue
BHIS248
BASN251
BASN252

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 409
ChainResidue
BSER63
BVAL65
BASN229

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
ALYS62
AASN229
AARG285
BLYS62
BASN229
BARG285

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

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon