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Yorodumi- PDB-1fid: STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fid | ||||||
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Title | STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT | ||||||
Components | GAMMA FIBRINOGEN | ||||||
Keywords | BLOOD COAGULATION FACTOR / BLOOD COAGULATION / GLYCOPROTEIN / CALCIUM / PLATELET / PLASMA / ALTERNATIVE SPLICING / DISEASE MUTATION / POLYMORPHISM | ||||||
Function / homology | Function and homology information platelet maturation / fibrinogen complex / Regulation of TLR by endogenous ligand / platelet alpha granule / blood coagulation, fibrin clot formation / cellular response to interleukin-6 / positive regulation of heterotypic cell-cell adhesion / MyD88 deficiency (TLR2/4) / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane ...platelet maturation / fibrinogen complex / Regulation of TLR by endogenous ligand / platelet alpha granule / blood coagulation, fibrin clot formation / cellular response to interleukin-6 / positive regulation of heterotypic cell-cell adhesion / MyD88 deficiency (TLR2/4) / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / extracellular matrix structural constituent / plasminogen activation / p130Cas linkage to MAPK signaling for integrins / positive regulation of peptide hormone secretion / positive regulation of exocytosis / GRB2:SOS provides linkage to MAPK signaling for Integrins / cellular response to interleukin-1 / protein polymerization / protein secretion / Integrin cell surface interactions / negative regulation of endothelial cell apoptotic process / Common Pathway of Fibrin Clot Formation / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / positive regulation of substrate adhesion-dependent cell spreading / cell adhesion molecule binding / positive regulation of vasoconstriction / fibrinolysis / Integrin signaling / cell-matrix adhesion / platelet alpha granule lumen / positive regulation of protein secretion / Post-translational protein phosphorylation / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / platelet aggregation / response to calcium ion / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / Platelet degranulation / ER-Phagosome pathway / protein-containing complex assembly / collagen-containing extracellular matrix / blood microparticle / positive regulation of ERK1 and ERK2 cascade / endoplasmic reticulum lumen / external side of plasma membrane / signaling receptor binding / structural molecule activity / cell surface / extracellular space / extracellular exosome / extracellular region / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Yee, V.C. / Teller, D.C. | ||||||
Citation | Journal: Structure / Year: 1997 Title: Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. Authors: Yee, V.C. / Pratt, K.P. / Cote, H.C. / Trong, I.L. / Chung, D.W. / Davie, E.W. / Stenkamp, R.E. / Teller, D.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fid.cif.gz | 67.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fid.ent.gz | 48.6 KB | Display | PDB format |
PDBx/mmJSON format | 1fid.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fid_validation.pdf.gz | 411.7 KB | Display | wwPDB validaton report |
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Full document | 1fid_full_validation.pdf.gz | 412.6 KB | Display | |
Data in XML | 1fid_validation.xml.gz | 14.3 KB | Display | |
Data in CIF | 1fid_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fi/1fid ftp://data.pdbj.org/pub/pdb/validation_reports/fi/1fid | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30243.422 Da / Num. of mol.: 1 / Fragment: 30 KD CARBOXYL TERMINAL FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HUMAN FIBRINOGEN GAMMA CHAIN C / Organ: BLOOD / Plasmid: PPIC9K Gene (production host): HUMAN FIBRINOGEN GAMMA CHAIN CDNA ENCODING VAL 143 - VAL 411 Production host: Pichia pastoris (fungus) / References: UniProt: P02679 |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 36 % | ||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6. | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: May 8, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 16754 / % possible obs: 94.6 % / Observed criterion σ(I): 0 / Redundancy: 6 % / Rmerge(I) obs: 0.061 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 50 Å |
-Processing
Software |
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Refinement | Resolution: 2.1→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 16 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.19 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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