Structure of PDB 4zel Chain A Binding Site BS01

Receptor Information
>4zel Chain A (length=550) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGEL
ENADLVVLWTDGDAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLL
FKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQ
LLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHI
IKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCR
HVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDS
SGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQ
LALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQE
IRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYP
QTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNS
FNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTVVS
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain4zel Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4zel The crystal structure of human dopamine beta-hydroxylase at 2.9 angstrom resolution.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		H412 M487
Binding residue
(residue number reindexed from 1)		H366 M441
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H262 H263 E331 H333 H412 H414 M487
Catalytic site (residue number reindexed from 1) H216 H217 E285 H287 H366 H368 M441
Enzyme Commision number 1.14.17.1: dopamine beta-monooxygenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004497 monooxygenase activity
GO:0004500 dopamine beta-monooxygenase activity
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0016715 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
Biological Process
GO:0001974 blood vessel remodeling
GO:0001975 response to amphetamine
GO:0002443 leukocyte mediated immunity
GO:0006589 octopamine biosynthetic process
GO:0007268 chemical synaptic transmission
GO:0007613 memory
GO:0007626 locomotory behavior
GO:0008306 associative learning
GO:0008542 visual learning
GO:0042309 homoiothermy
GO:0042310 vasoconstriction
GO:0042420 dopamine catabolic process
GO:0042421 norepinephrine biosynthetic process
GO:0042423 catecholamine biosynthetic process
GO:0042593 glucose homeostasis
GO:0042596 fear response
GO:0042711 maternal behavior
GO:0045907 positive regulation of vasoconstriction
GO:0048149 behavioral response to ethanol
GO:0048265 response to pain
GO:0050900 leukocyte migration
GO:0120162 positive regulation of cold-induced thermogenesis
GO:1904705 regulation of vascular associated smooth muscle cell proliferation
GO:1905562 regulation of vascular endothelial cell proliferation
GO:2001236 regulation of extrinsic apoptotic signaling pathway
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0016020 membrane
GO:0030658 transport vesicle membrane
GO:0030667 secretory granule membrane
GO:0031410 cytoplasmic vesicle
GO:0034451 centriolar satellite
GO:0034466 chromaffin granule lumen
GO:0034774 secretory granule lumen
GO:0042584 chromaffin granule membrane
GO:0043231 intracellular membrane-bounded organelle
GO:0045202 synapse

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4zel, PDBe:4zel, PDBj:4zel
PDBsum4zel
PubMed27152332
UniProtP09172|DOPO_HUMAN Dopamine beta-hydroxylase (Gene Name=DBH)

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