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- PDB-2aw0: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATP... -
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Basic information
Entry | Database: PDB / ID: 2aw0 | ||||||
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Title | FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES | ||||||
![]() | MENKES COPPER-TRANSPORTING ATPASE | ||||||
![]() | COPPER TRANSPORT / COPPER-TRANSPORTING ATPASE / COPPER-BINDING DOMAIN / HYDROLASE | ||||||
Function / homology | ![]() 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 / copper ion transmembrane transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / positive regulation of melanin biosynthetic process / copper ion export / superoxide dismutase copper chaperone activity / copper ion import / cellular response to lead ion / pyramidal neuron development / copper ion homeostasis / copper ion transport / melanosome membrane / catecholamine metabolic process / serotonin metabolic process / detoxification of copper ion / trans-Golgi network transport vesicle / norepinephrine metabolic process / regulation of oxidative phosphorylation / 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 / cellular response to antibiotic / skin development / hair follicle morphogenesis / positive regulation of catalytic activity / pigmentation / dopamine metabolic process / lung alveolus development / response to zinc ion / cellular response to platelet-derived growth factor stimulus / blood vessel development / Detoxification of Reactive Oxygen Species / cell leading edge / central nervous system neuron development / cuprous ion binding / Ion transport by P-type ATPases / microvillus / positive regulation of cell size / intracellular copper ion homeostasis / 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 / neuron projection morphogenesis / positive regulation of epithelial cell proliferation / trans-Golgi network membrane / liver development / mitochondrion organization / secretory granule / locomotory behavior / female pregnancy / cellular response to iron ion / brush border membrane / cellular response to amino acid stimulus / trans-Golgi network / small GTPase binding / phagocytic vesicle membrane / late endosome / protein-folding chaperone binding / early endosome membrane / cellular response to hypoxia / basolateral plasma membrane / perikaryon / 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 | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
![]() | Gitschier, J. / Fairbrother, W.J. | ||||||
![]() | ![]() Title: Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Authors: Gitschier, J. / Moffat, B. / Reilly, D. / Wood, W.I. / Fairbrother, W.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 414.9 KB | Display | ![]() |
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PDB format | ![]() | 345.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7636.557 Da / Num. of mol.: 1 / Fragment: FOURTH METAL-BINDING DOMAIN Source method: isolated from a genetically manipulated source Details: AG(I)-BOUND STATE / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-AG / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6.8 / Temperature: 300 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX500 / Manufacturer: Bruker / Model: AMX500 / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST RESIDUAL RESTRAINT VIOLATION ENERGIES Conformers calculated total number: 40 / Conformers submitted total number: 20 |