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Yorodumi- PDB-1hov: SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH ... -
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-Basic information
Entry | Database: PDB / ID: 1hov | ||||||
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Title | SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020 | ||||||
Components | MATRIX METALLOPROTEINASE-2 | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / enzyme-inhibitor complex / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information gelatinase A / peripheral nervous system axon regeneration / blood vessel maturation / parturition / luteinization / bone trabecula formation / tissue remodeling / intramembranous ossification / cellular response to UV-A / ovulation from ovarian follicle ...gelatinase A / peripheral nervous system axon regeneration / blood vessel maturation / parturition / luteinization / bone trabecula formation / tissue remodeling / intramembranous ossification / cellular response to UV-A / ovulation from ovarian follicle / positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / prostate gland epithelium morphogenesis / protein metabolic process / cellular response to fluid shear stress / negative regulation of cell adhesion / face morphogenesis / negative regulation of vasoconstriction / macrophage chemotaxis / Activation of Matrix Metalloproteinases / endodermal cell differentiation / response to amyloid-beta / fibronectin binding / Collagen degradation / collagen catabolic process / cellular response to interleukin-1 / extracellular matrix disassembly / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / response to hyperoxia / response to electrical stimulus / response to retinoic acid / response to mechanical stimulus / ovarian follicle development / positive regulation of vascular associated smooth muscle cell proliferation / cellular response to estradiol stimulus / embryo implantation / Degradation of the extracellular matrix / sarcomere / cellular response to amino acid stimulus / extracellular matrix organization / response to activity / cellular response to reactive oxygen species / response to nicotine / protein catabolic process / response to hydrogen peroxide / metalloendopeptidase activity / response to estrogen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / metallopeptidase activity / heart development / endopeptidase activity / Interleukin-4 and Interleukin-13 signaling / angiogenesis / collagen-containing extracellular matrix / Extra-nuclear estrogen signaling / response to hypoxia / positive regulation of cell migration / response to xenobiotic stimulus / serine-type endopeptidase activity / mitochondrion / proteolysis / extracellular space / zinc ion binding / extracellular region / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
Authors | Feng, Y. / Likos, J.J. / Zhu, L. / Woodward, H. / Munie, G. / McDonald, J.J. / Stevens, A.M. / Howard, C.P. / De Crescenzo, G.A. / Welsch, D. ...Feng, Y. / Likos, J.J. / Zhu, L. / Woodward, H. / Munie, G. / McDonald, J.J. / Stevens, A.M. / Howard, C.P. / De Crescenzo, G.A. / Welsch, D. / Shieh, H.-S. / Stallings, W.C. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2002 Title: Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor Authors: Feng, Y. / Likos, J.J. / Zhu, L. / Woodward, H. / Munie, G. / McDonald, J.J. / Stevens, A.M. / Howard, C.P. / De Crescenzo, G.A. / Welsch, D. / Shieh, H.-S. / Stallings, W.C. #1: Journal: J.Biomol.NMR / Year: 2000 Title: 1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2 | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hov.cif.gz | 572.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hov.ent.gz | 471.6 KB | Display | PDB format |
PDBx/mmJSON format | 1hov.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hov_validation.pdf.gz | 434.6 KB | Display | wwPDB validaton report |
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Full document | 1hov_full_validation.pdf.gz | 633.9 KB | Display | |
Data in XML | 1hov_validation.xml.gz | 65.2 KB | Display | |
Data in CIF | 1hov_validation.cif.gz | 81.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ho/1hov ftp://data.pdbj.org/pub/pdb/validation_reports/ho/1hov | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18491.391 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): W3110-II5 / References: UniProt: P08253, gelatinase A | ||||
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#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-I52 / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Details | Contents: 0.3-0.4mM U-15N, 13C MMP-2C: unlabeled SC-74020 in 20mM TRIS-d11-HCl, 5mM CaCl2, 10uM ZnCl2, 20uM unlabeled SC-74020 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50 / pH: 7.4 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: reasonable inhibitor conformation | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 14 / Conformers submitted total number: 11 |