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- PDB-1q8l: Second Metal Binding Domain of the Menkes ATPase -

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Basic information

Entry
Database: PDB / ID: 1q8l
TitleSecond Metal Binding Domain of the Menkes ATPase
ComponentsCopper-transporting ATPase 1
KeywordsMETAL BINDING PROTEIN
Function / homology
Function and homology information


peptidyl-lysine modification / epinephrine metabolic process / elastin biosynthetic process / positive regulation of response to wounding / tryptophan metabolic process / cellular response to cobalt ion / Ion influx/efflux at host-pathogen interface / positive regulation of tyrosinase activity / copper-dependent protein binding / cerebellar Purkinje cell differentiation ...peptidyl-lysine modification / epinephrine metabolic process / elastin biosynthetic process / positive regulation of response to wounding / tryptophan metabolic process / cellular response to cobalt ion / Ion influx/efflux at host-pathogen interface / positive regulation of tyrosinase activity / copper-dependent protein binding / cerebellar Purkinje cell differentiation / elastic fiber assembly / response to iron(III) ion / P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion export / copper ion import / copper ion transmembrane transporter activity / positive regulation of melanin biosynthetic process / superoxide dismutase copper chaperone activity / cellular response to lead ion / pyramidal neuron development / copper ion homeostasis / copper ion transport / melanosome membrane / serotonin metabolic process / catecholamine metabolic process / detoxification of copper ion / regulation of oxidative phosphorylation / trans-Golgi network transport vesicle / norepinephrine metabolic process / T-helper cell differentiation / positive regulation of vascular associated smooth muscle cell migration / collagen fibril organization / cartilage development / response to manganese ion / negative regulation of iron ion transmembrane transport / pigmentation / cellular response to antibiotic / skin development / hair follicle morphogenesis / dopamine metabolic process / lung alveolus development / response to zinc ion / cellular response to platelet-derived growth factor stimulus / positive regulation of catalytic activity / central nervous system neuron development / blood vessel development / Detoxification of Reactive Oxygen Species / cuprous ion binding / cell leading edge / microvillus / Ion transport by P-type ATPases / intracellular copper ion homeostasis / positive regulation of cell size / blood vessel remodeling / positive regulation of lamellipodium assembly / cellular response to copper ion / cellular response to cadmium ion / lactation / removal of superoxide radicals / extracellular matrix organization / mitochondrion organization / neuron projection morphogenesis / trans-Golgi network membrane / locomotory behavior / liver development / secretory granule / female pregnancy / positive regulation of epithelial cell proliferation / brush border membrane / cellular response to amino acid stimulus / trans-Golgi network / cellular response to iron ion / small GTPase binding / phagocytic vesicle membrane / late endosome / cellular response to hypoxia / protein-folding chaperone binding / perikaryon / early endosome membrane / basolateral plasma membrane / in utero embryonic development / postsynaptic density / neuron projection / apical plasma membrane / copper ion binding / axon / neuronal cell body / dendrite / perinuclear region of cytoplasm / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / ATP binding / membrane / plasma membrane / cytosol
Similarity search - Function
Heavy metal-associated domain, copper ion-binding / P-type ATPase, subfamily IB / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / E1-E2 ATPase ...Heavy metal-associated domain, copper ion-binding / P-type ATPase, subfamily IB / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / E1-E2 ATPase / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site / P-type ATPase, cytoplasmic domain N / E1-E2 ATPases phosphorylation site. / P-type ATPase, A domain superfamily / P-type ATPase / P-type ATPase, transmembrane domain superfamily / haloacid dehalogenase-like hydrolase / HAD superfamily / HAD-like superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Copper-transporting ATPase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / molecular dynamics
AuthorsJones, C.E. / Daly, N.L. / Cobine, P.A. / Craik, D.J. / Dameron, C.T.
CitationJournal: J.Struct.Biol. / Year: 2003
Title: Structure and metal binding studies of the second copper binding domain of the Menkes ATPase.
Authors: Jones, C.E. / Daly, N.L. / Cobine, P.A. / Craik, D.J. / Dameron, C.T.
History
DepositionAug 21, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 20, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Copper-transporting ATPase 1


Theoretical massNumber of molelcules
Total (without water)9,3091
Polymers9,3091
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Copper-transporting ATPase 1 / Copper pump 1 / Menkes disease-associated protein


Mass: 9309.011 Da / Num. of mol.: 1 / Fragment: Second Copper Binding Domain (residues 164-246)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ATP7A OR MNK OR MC1 / Plasmid: pET29-a / Production host: Escherichia coli (E. coli) / References: UniProt: Q04656

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
1313D 15N-separated NOESY
141DQF-COSY
1513D 15N-seperated TOCSY

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Sample preparation

DetailsContents: 0.5mM MNKr2, U-15N, 20mM potassium phosphate, 10 mM Sodium Chloride, pH6.5.
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 30mM / pH: 6.5 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851Brugner A. Trefinement
DYANA1.5Guntert, Pstructure solution
XEASY3.2Bartels, Cdata analysis
RefinementMethod: molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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