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Yorodumi- PDB-1brq: CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1brq | ||||||
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Title | CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BINDING PROTEIN AT 2.5 ANGSTROMS RESOLUTION | ||||||
Components | RETINOL BINDING PROTEIN | ||||||
Keywords | RETINOL TRANSPORT | ||||||
Function / homology | Function and homology information Retinoid metabolism disease events / urinary bladder development / embryonic retina morphogenesis in camera-type eye / retinol transport / female genitalia morphogenesis / retinol transmembrane transporter activity / embryonic organ morphogenesis / maintenance of gastrointestinal epithelium / embryonic skeletal system development / negative regulation of cardiac muscle cell proliferation ...Retinoid metabolism disease events / urinary bladder development / embryonic retina morphogenesis in camera-type eye / retinol transport / female genitalia morphogenesis / retinol transmembrane transporter activity / embryonic organ morphogenesis / maintenance of gastrointestinal epithelium / embryonic skeletal system development / negative regulation of cardiac muscle cell proliferation / eye development / heart trabecula formation / retinal binding / cardiac muscle tissue development / retinol metabolic process / retinol binding / positive regulation of immunoglobulin production / Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / uterus development / vagina development / response to retinoic acid / Retinoid metabolism and transport / visual perception / gluconeogenesis / lung development / positive regulation of insulin secretion / glucose homeostasis / heart development / extracellular space / extracellular exosome / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Zanotti, G. / Monaco, H.L. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1993 Title: Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 A resolution. Authors: Zanotti, G. / Ottonello, S. / Berni, R. / Monaco, H.L. #1: Journal: J.Mol.Biol. / Year: 1984 Title: Crystallization of Human Plasma Apo-Retinol-Binding Protein Authors: Monaco, H.L. / Zanotti, G. / Ottonello, S. / Berni, R. #2: Journal: J.Mol.Biol. / Year: 1983 Title: Crystallization and Preliminary X-Ray Data of Human Plasma Retinol-Binding Protein Authors: Ottonello, S. / Maraini, G. / Mammi, M. / Monaco, H.L. / Spadon, P. / Zanotti, G. | ||||||
History |
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Remark 700 | SHEET THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1brq.cif.gz | 48.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1brq.ent.gz | 34.4 KB | Display | PDB format |
PDBx/mmJSON format | 1brq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1brq_validation.pdf.gz | 366.4 KB | Display | wwPDB validaton report |
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Full document | 1brq_full_validation.pdf.gz | 382.2 KB | Display | |
Data in XML | 1brq_validation.xml.gz | 7 KB | Display | |
Data in CIF | 1brq_validation.cif.gz | 9.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/br/1brq ftp://data.pdbj.org/pub/pdb/validation_reports/br/1brq | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: DISORDERED AREAS: RESIDUES 1 - 3, 64 - 67, AND C TERMINAL PORTION (RESIDUES 175 - 182) CANNOT BE SEEN IN THE MAP. |
-Components
#1: Protein | Mass: 20984.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P02753 |
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#2: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.83 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: microdialysis | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 9999 Å / Num. obs: 9776 / Num. measured all: 19031 / Rmerge(I) obs: 0.107 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.7 Å / % possible obs: 75 % / Num. measured obs: 1554 |
-Processing
Software |
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Refinement | Highest resolution: 2.5 Å /
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Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 9 Å / Num. reflection obs: 9614 / Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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