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- PDB-1cfa: SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cfa | ||||||
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Title | SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES | ||||||
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![]() | Immune system/INHIBITOR / COMPLEMENT FACTOR / COMPLEMENT ALTERNATE PATHWAY / GLYCOPROTEIN / AGGREGATION INHIBITOR / GP ANTAGONIST / COMPLEMENT FACTOR-PEPTIDE complex / Immune system-INHIBITOR complex | ||||||
Function / homology | ![]() Terminal pathway of complement / membrane attack complex / Activation of C3 and C5 / negative regulation of macrophage chemotaxis / complement activation, alternative pathway / chemokine activity / endopeptidase inhibitor activity / positive regulation of vascular endothelial growth factor production / positive regulation of chemokine production / Peptide ligand-binding receptors ...Terminal pathway of complement / membrane attack complex / Activation of C3 and C5 / negative regulation of macrophage chemotaxis / complement activation, alternative pathway / chemokine activity / endopeptidase inhibitor activity / positive regulation of vascular endothelial growth factor production / positive regulation of chemokine production / Peptide ligand-binding receptors / complement activation, classical pathway / Regulation of Complement cascade / chemotaxis / G alpha (i) signalling events / killing of cells of another organism / cell surface receptor signaling pathway / inflammatory response / G protein-coupled receptor signaling pathway / signaling receptor binding / extracellular space / extracellular exosome / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Zhang, X. / Boyar, W. / Galakatos, N. / Gonnella, N.C. | ||||||
![]() | ![]() Title: Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding. Authors: Zhang, X. / Boyar, W. / Galakatos, N. / Gonnella, N.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 459.2 KB | Display | ![]() |
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PDB format | ![]() | 378.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 353.8 KB | Display | ![]() |
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Full document | ![]() | 613.5 KB | Display | |
Data in XML | ![]() | 66.3 KB | Display | |
Data in CIF | ![]() | 88.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7950.314 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 71 / Mutation: Q71C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 448.561 Da / Num. of mol.: 1 / Fragment: RESIDUES 72 - 75 Source method: isolated from a genetically manipulated source |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 5.2 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 20 |