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

2NNH

CYP2C8dH complexed with 2 molecules of 9-cis retinoic acid

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
B0002933biological_processlipid hydroxylation
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006082biological_processorganic acid metabolic process
B0006629biological_processlipid metabolic process
B0006721biological_processterpenoid metabolic process
B0006805biological_processxenobiotic metabolic process
B0008202biological_processsteroid metabolic process
B0008210biological_processestrogen metabolic process
B0008392molecular_functionarachidonate epoxygenase activity
B0008401molecular_functionretinoic acid 4-hydroxylase activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016712molecular_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
B0019369biological_processarachidonate metabolic process
B0019373biological_processepoxygenase P450 pathway
B0020037molecular_functionheme binding
B0032787biological_processmonocarboxylic acid metabolic process
B0034875molecular_functioncaffeine oxidase activity
B0042178biological_processxenobiotic catabolic process
B0042572biological_processretinol metabolic process
B0042573biological_processretinoic acid metabolic process
B0042759biological_processlong-chain fatty acid biosynthetic process
B0046456biological_processicosanoid biosynthetic process
B0046872molecular_functionmetal ion binding
B0070989biological_processoxidative demethylation
B0097267biological_processomega-hydroxylase P450 pathway
B0101020molecular_functionestrogen 16-alpha-hydroxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BARG132
BASN133

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AARG132
AASN133

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AALA297
AGLY298
ATHR301
ATHR302
ATHR305
ALEU361
AVAL366
AHIS368
APRO427
APHE428
ASER429
AARG433
ACYS435
ALEU440
AALA441
A9CR501
AARG97
AILE112
ATRP120
AARG124
AILE178

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG97
BILE112
BILE113
BTRP120
BARG124
BALA297
BGLY298
BTHR301
BTHR302
BTHR305
BGLN356
BLEU361
BVAL366
BHIS368
BPRO427
BPHE428
BSER429
BARG433
BCYS435
B9CR501

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 9CR A 501
ChainResidue
AARG97
AGLY98
AASN99
ASER100
ASER103
AILE113
ATHR301
AVAL366
AHEM500
A9CR502
AHOH541

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 9CR A 502
ChainResidue
ASER100
AASN204
ALEU208
AASN217
AVAL237
AARG241
AVAL296
AILE476
A9CR501

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 9CR B 501
ChainResidue
BGLY98
BASN99
BSER100
BILE113
BTHR301
BVAL366
BPRO367
BHEM500
B9CR502
BHOH534

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 9CR B 502
ChainResidue
BSER100
BASN204
BLEU208
BARG241
BVAL296
BILE476
B9CR501

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLM B 503
ChainResidue
AARG105
AILE106
ATRP212
ACYS216
ATHR229
AHOH535
BPHE226
BPRO227
BGLY228
BTHR229

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLM A 503
ChainResidue
BPHE226
BHIS230
BLEU234
APHE226
APRO227
AGLY228
ATHR229
BILE102
BILE106
BTRP212

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 Residues6
DetailsBINDING:
ChainResidueDetails
ASER100
AASN204
AARG241
BSER100
BASN204
BARG241

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS435
BCYS435

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER100
BSER100

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU300
BTHR301

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon