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Yorodumi- PDB-1aw0: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATP... -
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-Basic information
Entry | Database: PDB / ID: 1aw0 | ||||||
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Title | FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES | ||||||
Components | MENKES COPPER-TRANSPORTING ATPASE | ||||||
Keywords | HYDROLASE / COPPER-TRANSPORTING ATPASE / COPPER-BINDING DOMAIN | ||||||
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 | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Gitschier, J. / Fairbrother, W.J. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1998 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1aw0.cif.gz | 416.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1aw0.ent.gz | 349.5 KB | Display | PDB format |
PDBx/mmJSON format | 1aw0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aw/1aw0 ftp://data.pdbj.org/pub/pdb/validation_reports/aw/1aw0 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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: REDUCED APO STATE / Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q04656, EC: 3.6.1.36 |
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-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 |