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- SASDFN4: Domain-stapled mutant of Matrix metalloproteinase-1 (MMP-1 S243C,... -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDFN4
SampleDomain-stapled mutant of Matrix metalloproteinase-1 (MMP-1 S243C, S318C)
  • Matrix metalloproteinase-1 (Interstitial collagenase) (S243C, S318C) (protein), MMP-1 (S243C, S318C), Homo sapiens
Function / homology
Function and homology information


interstitial collagenase / cellular response to UV-A / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix ...interstitial collagenase / cellular response to UV-A / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / positive regulation of protein-containing complex assembly / metalloendopeptidase activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / peptidase activity / Interleukin-4 and Interleukin-13 signaling / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular region / zinc ion binding
Similarity search - Function
Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain / Peptidoglycan binding-like / Peptidase M10A, cysteine switch, zinc binding site / Matrixins cysteine switch. / Hemopexin-like repeats / Hemopexin-like domain superfamily / Hemopexin / Putative peptidoglycan binding domain ...Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain / Peptidoglycan binding-like / Peptidase M10A, cysteine switch, zinc binding site / Matrixins cysteine switch. / Hemopexin-like repeats / Hemopexin-like domain superfamily / Hemopexin / Putative peptidoglycan binding domain / Hemopexin repeat profile. / Hemopexin-like repeats. / Peptidase M10A / Peptidase M10A, catalytic domain / Peptidase M10, metallopeptidase / Matrixin / PGBD-like superfamily / Peptidase, metallopeptidase / Zinc-dependent metalloprotease / Metallopeptidase, catalytic domain superfamily / Neutral zinc metallopeptidases, zinc-binding region signature.
Similarity search - Domain/homology
Interstitial collagenase
Similarity search - Component
Biological speciesHomo sapiens (human)
Contact author
  • Rob Holland (University of Portsmouth)

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Structure visualization

Downloads & links

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Models

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Sample

SampleName: Domain-stapled mutant of Matrix metalloproteinase-1 (MMP-1 S243C, S318C)
Specimen concentration: 8 mg/ml
BufferName: 50 mM Tris-HCl, 150 mM Sodium chloride, 10 mM Calcium chloride
pH: 7.4
Entity #1571Name: MMP-1 (S243C, S318C) / Type: protein
Description: Matrix metalloproteinase-1 (Interstitial collagenase) (S243C, S318C)
Formula weight: 42.666 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P03956
Sequence: FVLTEGNPRW EQTHLTYRIE NYTPDLPRAD VDHAIEKAFQ LWSNVTPLTF TKVSEGQADI MISFVRGDHR DNSPFDGPGG NLAHAFQPGP GIGGDAHFDE DERWTNNFRE YNLHRVAAHE LGHSLGLSHS TDIGALMYPS YTFCGDVQLA QDDIDGIQAI YGRSQNPVQP ...Sequence:
FVLTEGNPRW EQTHLTYRIE NYTPDLPRAD VDHAIEKAFQ LWSNVTPLTF TKVSEGQADI MISFVRGDHR DNSPFDGPGG NLAHAFQPGP GIGGDAHFDE DERWTNNFRE YNLHRVAAHE LGHSLGLSHS TDIGALMYPS YTFCGDVQLA QDDIDGIQAI YGRSQNPVQP IGPQTPKACD SKLTFDAITT IRGEVMFFKD RFYMRTNPFY PEVELNFICV FWPQLPNGLE AAYEFADRDE VRFFKGNKYW AVQGQNVLHG YPKDIYSSFG FPRTVKHIDA ALSEENTGKT YFFVANKYWR YDEYKRSMDP GYPKMIAHDF PGIGHKVDAV FMKDGFFYFF HGTRQYKFDP KTKRILTLQK ANSWFNCRKN

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Experimental information

BeamInstrument name: Diamond Light Source B21 / City: Oxfordshire / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 3.9 mm
DetectorName: Pilatus 2M
Scan
Title: Domain-stapled mutant of Matrix metalloproteinase-1 (MMP-1 S243C, S318C)
Measurement date: May 14, 2016 / Storage temperature: 4 °C / Cell temperature: 25 °C / Exposure time: 3 sec. / Number of frames: 29 / Unit: 1/A /
MinMax
Q0.004 0.4078
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 880 /
MinMax
Q0.00951241 0.251124
P(R) point1 880
R0 77
Result
Type of curve: sec /
ExperimentalPorod
MW33.825 kDa29 kDa
Volume-46 nm3

P(R)GuinierGuinier error
Forward scattering, I00.001545 0.001574 1.2E-5
Radius of gyration, Rg2.5 nm2.562 nm0.033

MinMax
D-7.7
Guinier point21 169

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