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- PDB-1elv: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S... -
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Basic information
Entry | Database: PDB / ID: 1elv | |||||||||
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Title | CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE | |||||||||
![]() | COMPLEMENT C1S COMPONENT | |||||||||
![]() | HYDROLASE / TRYPSIN-LIKE SERIN PROTEASE / CCP (OR SUSHI OR SCR)MODULE | |||||||||
Function / homology | ![]() complement subcomponent C_overbar_1s_ / Classical antibody-mediated complement activation / Initial triggering of complement / complement activation, classical pathway / Regulation of Complement cascade / blood microparticle / serine-type endopeptidase activity / innate immune response / calcium ion binding / proteolysis ...complement subcomponent C_overbar_1s_ / Classical antibody-mediated complement activation / Initial triggering of complement / complement activation, classical pathway / Regulation of Complement cascade / blood microparticle / serine-type endopeptidase activity / innate immune response / calcium ion binding / proteolysis / extracellular space / extracellular region / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Gaboriaud, C. / Rossi, V. / Bally, I. / Arlaud, G. / Fontecilla-Camps, J.-C. | |||||||||
![]() | ![]() Title: Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle. Authors: Gaboriaud, C. / Rossi, V. / Bally, I. / Arlaud, G.J. / Fontecilla-Camps, J.C. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.7 KB | Display | ![]() |
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PDB format | ![]() | 62 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-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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Unit cell |
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Components
#1: Protein | Mass: 36687.473 Da / Num. of mol.: 1 Fragment: CCP2-SP CATALYTIC FRAGMENT: ASP363-ASP-673 SEGMENT PRECEDED BY AN ASP-LEU SEQUENCE ADDED AT THE N-TERMINAL END Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P09871, complement subcomponent C_overbar_1s_ | ||||
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
#3: Chemical | #4: Chemical | ChemComp-NES / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.8 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PEG 4K 34%, AMMONIUM SULFATE 100mM, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 24, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→15 Å / Num. all: 39489 / Num. obs: 115710 / % possible obs: 93 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 21.7 Å2 / Rsym value: 0.037 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 1.7→1.75 Å / Redundancy: 1.5 % / Mean I/σ(I) obs: 3.4 / Rsym value: 0.247 / % possible all: 75.8 |
Reflection | *PLUS Num. obs: 39489 / Num. measured all: 115710 / Rmerge(I) obs: 0.037 |
Reflection shell | *PLUS % possible obs: 75.8 % / Rmerge(I) obs: 0.247 |
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Processing
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Refinement | Resolution: 1.7→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Lamzin (arp.dic) Details: LIKELY BECAUSE OF RADIATION DAMAGES, THE INTERCHAIN DISULFIDE BRIDGE (A410-A534) IS NOT FORMED, SEVERAL CYSTEINES ARE OBSERVED WITH DUAL CONFORMATION (A371, A410, A580, A613) AND DENSITY IS ...Details: LIKELY BECAUSE OF RADIATION DAMAGES, THE INTERCHAIN DISULFIDE BRIDGE (A410-A534) IS NOT FORMED, SEVERAL CYSTEINES ARE OBSERVED WITH DUAL CONFORMATION (A371, A410, A580, A613) AND DENSITY IS LACKING AT THE END OF SEVERAL GLU (A351, A359, A372, A373, A385, A397, A402, A506), ASP (A357, A541), LYS (A629) AND MET (A545) RESIDUES. (THIS IS BRIEFLY DISCUSSED IN THE ABOVE REFERENCE).
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Displacement parameters | Biso mean: 26.7 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 15 Å / σ(F): 0 / Rfactor obs: 0.185 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 26.7 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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