Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2NNI

CYP2C8dH complexed with montelukast

Functional Information from GO Data
ChainGOidnamespacecontents
A0002933biological_processlipid hydroxylation
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006082biological_processorganic acid metabolic process
A0006629biological_processlipid metabolic process
A0006721biological_processterpenoid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008210biological_processestrogen metabolic process
A0008392molecular_functionarachidonate epoxygenase activity
A0008401molecular_functionretinoic acid 4-hydroxylase activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A0019369biological_processarachidonate metabolic process
A0019373biological_processepoxygenase P450 pathway
A0020037molecular_functionheme binding
A0032787biological_processmonocarboxylic acid metabolic process
A0034875molecular_functioncaffeine oxidase activity
A0042178biological_processxenobiotic catabolic process
A0042572biological_processretinol metabolic process
A0042573biological_processretinoic acid metabolic process
A0042759biological_processlong-chain fatty acid biosynthetic process
A0046456biological_processicosanoid biosynthetic process
A0046872molecular_functionmetal ion binding
A0070989biological_processoxidative demethylation
A0097267biological_processomega-hydroxylase P450 pathway
A0101020molecular_functionestrogen 16-alpha-hydroxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG132
AASN133

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AGLY298
ATHR301
ATHR302
ATHR305
AVAL366
AHIS368
APRO427
APHE428
ASER429
AARG433
ACYS435
AGLY437
AALA441
AARG97
AILE112
AILE113
ATRP120
AARG124
ALEU294
AALA297

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE MTK A 501
ChainResidue
ASER100
ASER103
AILE106
ATHR107
AILE113
ASER114
AARG200
APHE201
AASN204
ALEU208
AILE213
AASN217
AASN236
AVAL237
ATHR240
AVAL296
AALA297
ATHR301
AVAL477

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PLM A 502
ChainResidue
AARG105
AILE106
APHE226
APRO227
AGLY228
ATHR229
ATHR229
AHIS230
ALEU234

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSaGKRICAG
ChainResidueDetails
APHE428-GLY437

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ASER100
AASN204
AARG241

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS435

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER100

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU300
ATHR301

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon