[English] 日本語
Yorodumi- PDB-1btt: THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1btt | ||||||
---|---|---|---|---|---|---|---|
Title | THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3 | ||||||
Components | BAND 3 ANION TRANSPORT PROTEIN | ||||||
Keywords | TRANSMEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / Bicarbonate transporters / intracellular monoatomic ion homeostasis / ankyrin-1 complex / plasma membrane phospholipid scrambling / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity ...pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / Bicarbonate transporters / intracellular monoatomic ion homeostasis / ankyrin-1 complex / plasma membrane phospholipid scrambling / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / bicarbonate transport / bicarbonate transmembrane transporter activity / monoatomic anion transport / chloride transport / chloride transmembrane transporter activity / ankyrin binding / negative regulation of glycolytic process through fructose-6-phosphate / hemoglobin binding / cortical cytoskeleton / erythrocyte development / protein-membrane adaptor activity / chloride transmembrane transport / protein localization to plasma membrane / regulation of intracellular pH / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / cytoplasmic side of plasma membrane / transmembrane transport / Z disc / blood coagulation / basolateral plasma membrane / blood microparticle / protein homodimerization activity / extracellular exosome / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Gargaro, A.R. / Bloomberg, G.B. / Dempsey, C.E. / Murray, M. / Tanner, M.J.A. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 1994 Title: The solution structures of the first and second transmembrane-spanning segments of band 3. Authors: Gargaro, A.R. / Bloomberg, G.B. / Dempsey, C.E. / Murray, M. / Tanner, M.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1btt.cif.gz | 117.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1btt.ent.gz | 92.5 KB | Display | PDB format |
PDBx/mmJSON format | 1btt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1btt_validation.pdf.gz | 336.1 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1btt_full_validation.pdf.gz | 425.8 KB | Display | |
Data in XML | 1btt_validation.xml.gz | 7.8 KB | Display | |
Data in CIF | 1btt_validation.cif.gz | 12.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/1btt ftp://data.pdbj.org/pub/pdb/validation_reports/bt/1btt | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 2096.491 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P02730 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-Processing
Software |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 21 |