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- PDB-1g5w: SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN -
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Open data
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Basic information
Entry | Database: PDB / ID: 1g5w | ||||||
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Title | SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN | ||||||
![]() | FATTY ACID-BINDING PROTEIN | ||||||
![]() | LIPID BINDING PROTEIN / NMR spectroscopy / protein-ligand interactions / selected-fit binding | ||||||
Function / homology | ![]() positive regulation of long-chain fatty acid import into cell / regulation of phosphatidylcholine biosynthetic process / regulation of fatty acid oxidation / positive regulation of phospholipid biosynthetic process / intracellular lipid transport / oleic acid binding / phospholipid homeostasis / long-chain fatty acid binding / Triglyceride catabolism / long-chain fatty acid transport ...positive regulation of long-chain fatty acid import into cell / regulation of phosphatidylcholine biosynthetic process / regulation of fatty acid oxidation / positive regulation of phospholipid biosynthetic process / intracellular lipid transport / oleic acid binding / phospholipid homeostasis / long-chain fatty acid binding / Triglyceride catabolism / long-chain fatty acid transport / brown fat cell differentiation / cytoskeletal protein binding / cholesterol homeostasis / negative regulation of cell population proliferation / extracellular space / extracellular exosome / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, energy-minimization | ||||||
![]() | Luecke, C. / Rademacher, M. / Zimmerman, A. / van Moerkerk, H.T.B. / Veerkamp, J.H. / Rueterjans, H. | ||||||
![]() | ![]() Title: Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Authors: Lucke, C. / Rademacher, M. / Zimmerman, A.W. / van Moerkerk, H.T. / Veerkamp, J.H. / Ruterjans, H. #1: ![]() Title: Three-dimensional structure of recombinant human muscle fatty acid-binding protein Authors: Zanotti, G. / Scapin, G. / Spandon, P. / Veerkamp, J.H. / Sacchettini, J.C. #2: ![]() Title: Structural studies on human muscle fatty acid-binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids Authors: Young, A.C.M. / Scapin, G. / Kromminga, A. / Patel, S.B. / Veerkamp, J.H. / Sacchettini, J.C. #3: ![]() Title: Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy Authors: Lassen, D. / Luecke, C. / Kveder, M. / Mesgarzadeh, A. / Schmidt, J.M. / Specht, B. / Lezius, A. / Spener, F. / Rueterjans, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 820.8 KB | Display | ![]() |
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PDB format | ![]() | 680.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 359.6 KB | Display | ![]() |
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Full document | ![]() | 456.6 KB | Display | |
Data in XML | ![]() | 53 KB | Display | |
Data in CIF | ![]() | 71.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 14747.825 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using non-delipidated recombinant human H-FABP samples. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 20 / pH: 5.5 / Pressure: ambient / Temperature: 310 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, energy-minimization / Software ordinal: 1 Details: The structure was determined based on 2589 NOE-derived distance constraints and 40 H-bond constraints. | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with lowest violations of experimental constraints Conformers calculated total number: 100 / Conformers submitted total number: 20 |