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

4ZEL

Human dopamine beta-hydroxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004497molecular_functionmonooxygenase activity
A0004500molecular_functiondopamine beta-monooxygenase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0006589biological_processoctopamine biosynthetic process
A0007268biological_processchemical synaptic transmission
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016715molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
A0030658cellular_componenttransport vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0031410cellular_componentcytoplasmic vesicle
A0031418molecular_functionL-ascorbic acid binding
A0034466cellular_componentchromaffin granule lumen
A0034774cellular_componentsecretory granule lumen
A0042420biological_processdopamine catabolic process
A0042421biological_processnorepinephrine biosynthetic process
A0042423biological_processcatecholamine biosynthetic process
A0042584cellular_componentchromaffin granule membrane
A0045202cellular_componentsynapse
A0046872molecular_functionmetal ion binding
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0003824molecular_functioncatalytic activity
B0004497molecular_functionmonooxygenase activity
B0004500molecular_functiondopamine beta-monooxygenase activity
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0006589biological_processoctopamine biosynthetic process
B0007268biological_processchemical synaptic transmission
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016715molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
B0030658cellular_componenttransport vesicle membrane
B0030667cellular_componentsecretory granule membrane
B0031410cellular_componentcytoplasmic vesicle
B0031418molecular_functionL-ascorbic acid binding
B0034466cellular_componentchromaffin granule lumen
B0034774cellular_componentsecretory granule lumen
B0042420biological_processdopamine catabolic process
B0042421biological_processnorepinephrine biosynthetic process
B0042423biological_processcatecholamine biosynthetic process
B0042584cellular_componentchromaffin granule membrane
B0045202cellular_componentsynapse
B0046872molecular_functionmetal ion binding
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00084
Number of Residues8
DetailsCU2_MONOOXYGENASE_1 Copper type II, ascorbate-dependent monooxygenases signature 1. HHMevFqC
ChainResidueDetails
AHIS262-CYS269

site_idPS00085
Number of Residues13
DetailsCU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HiFasqlHTHltG
ChainResidueDetails
AHIS405-GLY417

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27152332","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27152332","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZEL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"27152332","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZEL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27152332","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZEL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon