+Open data
-Basic information
Entry | Database: PDB / ID: 2rlq | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of CCP modules 2-3 of complement factor H | ||||||
Components | Complement factor HFactor H | ||||||
Keywords | IMMUNE SYSTEM / Complement / Factor H / Age-related macular degeneration / cofactor activity / Alternative splicing / Complement alternate pathway / Disease mutation / Glycoprotein / Immune response / Innate immunity / Polymorphism / Secreted / Sushi | ||||||
Function / homology | Function and homology information regulation of complement activation, alternative pathway / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / Regulation of Complement cascade ...regulation of complement activation, alternative pathway / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / Regulation of Complement cascade / heparin binding / blood microparticle / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / molecular dynamics, simulated annealing | ||||||
Authors | Hocking, H.G. / Herbert, A.P. / Pangburn, M.K. / Kavanagh, D. / Barlow, P.N. / Uhrin, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2008 Title: Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations. Authors: Hocking, H.G. / Herbert, A.P. / Kavanagh, D. / Soares, D.C. / Ferreira, V.P. / Pangburn, M.K. / Uhrin, D. / Barlow, P.N. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2rlq.cif.gz | 1014.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2rlq.ent.gz | 880.1 KB | Display | PDB format |
PDBx/mmJSON format | 2rlq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/2rlq ftp://data.pdbj.org/pub/pdb/validation_reports/rl/2rlq | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14183.697 Da / Num. of mol.: 1 / Fragment: residues in database 84-206 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CFH, HF, HF1, HF2 / Production host: Pichia pastoris (fungus) / Strain (production host): KM71H / References: UniProt: P08603 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sample conditions | pH: 6.2 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: molecular dynamics, simulated annealing / Software ordinal: 1 / Details: with simulated annealing | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 29 |