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- PDB-1rtg: C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rtg | ||||||
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Title | C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2 | ||||||
![]() | HUMAN GELATINASE A | ||||||
![]() | METALLOPROTEASE / MATRIX METALLO PROTEINASE (MMP) / GELATINASE / METZINCINS | ||||||
Function / homology | ![]() 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 / embryo implantation / Degradation of the extracellular matrix / sarcomere / extracellular matrix organization / response to activity / cellular response to estradiol stimulus / cellular response to amino acid stimulus / response to nicotine / protein catabolic process / response to hydrogen peroxide / metalloendopeptidase activity / cellular response to reactive oxygen species / 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 / Interleukin-4 and Interleukin-13 signaling / angiogenesis / collagen-containing extracellular matrix / endopeptidase activity / 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 | ![]() | ||||||
Method | ![]() | ||||||
![]() | Gohlke, U. / Bode, W. | ||||||
![]() | ![]() Title: The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. Authors: Gohlke, U. / Gomis-Ruth, F.X. / Crabbe, T. / Murphy, G. / Docherty, A.J. / Bode, W. #1: ![]() Title: A Helping Hand for Collagenases: The Haemopexin-Like Domain Authors: Bode, W. #2: ![]() Title: Structure of Full-Length Porcine Synovial Collagenase Reveals a C-Terminal Domain Containing a Calcium-Linked, Four-Bladed Beta-Propeller Authors: Li, J. / Brick, P. / O'Hare, M.C. / Skarzynski, T. / Lloyd, L.F. / Curry, V.A. / Clark, I.M. / Bigg, H.F. / Hazleman, B.L. / Cawston, T.E. / al., et | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.3 KB | Display | ![]() |
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PDB format | ![]() | 39.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Details | THERE IS ONE OLIGOTRIMER PRESENT IN THE ASYMMETRIC UNIT, I.E., ONE PROCARBOXYPEPTIDASE A MOLECULE, ONE PRO-PROTEINASE E MOLECULE, AND ONE CHYMOTRYPSINOGEN. |
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Components
#1: Protein | Mass: 23826.221 Da / Num. of mol.: 1 Fragment: C-TERMINAL RESIDUES 451 - 660, HAEMOPEXIN-LIKE DOMAIN Source method: isolated from a natural source / Source: (natural) ![]() | ||
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#2: Chemical | ChemComp-CL / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.63 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 9618 / % possible obs: 96.7 % / Rmerge(I) obs: 0.069 |
Reflection | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 9999 Å / Num. measured all: 34708 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.65 Å / % possible obs: 71.3 % / Rmerge(I) obs: 0.274 |
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Processing
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Refinement | Resolution: 2.6→8 Å /
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Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 19.1 Å2 |