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- PDB-1bzk: STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL... -

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Entry
Database: PDB / ID: 1bzk
TitleSTRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.
ComponentsPROTEIN (BAND 3 ANION TRANSPORT PROTEIN)
KeywordsTRANSPORT PROTEIN / HUMAN ERYTHROCYTE ANION TRANSPORTER / TRANSMEMBRANE / SYNTHETIC PEPTIDE
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 transmembrane transporter activity / bicarbonate transport / monoatomic anion transport / chloride transmembrane transporter activity / chloride transport / erythrocyte development / negative regulation of glycolytic process through fructose-6-phosphate / ankyrin binding / hemoglobin binding / cortical cytoskeleton / 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 / transmembrane transport / cytoplasmic side of plasma membrane / Z disc / blood coagulation / basolateral plasma membrane / blood microparticle / protein homodimerization activity / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Helical hairpin bin / Anion exchange protein 1 / Anion exchange protein / Anion exchange, conserved site / Anion exchangers family signature 1. / Anion exchangers family signature 2. / Band 3 cytoplasmic domain / Band 3 cytoplasmic domain / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain ...Helical hairpin bin / Anion exchange protein 1 / Anion exchange protein / Anion exchange, conserved site / Anion exchangers family signature 1. / Anion exchangers family signature 2. / Band 3 cytoplasmic domain / Band 3 cytoplasmic domain / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain / HCO3- transporter family / Phosphotransferase/anion transporter / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Band 3 anion transport protein
Similarity search - Component
MethodSOLUTION NMR / simulated annealing
AuthorsChambers, E.J. / Bloomberg, G.B. / Ring, S.M. / Tanner, M.J.A.
Citation
Journal: J.Mol.Biol. / Year: 1999
Title: Structural studies on the effects of the deletion in the red cell anion exchanger (band 3, AE1) associated with South East Asian ovalocytosis.
Authors: Chambers, E.J. / Bloomberg, G.B. / Ring, S.M. / Tanner, M.J.
#1: Journal: Biochem.Soc.Trans. / Year: 1998
Title: Studies on the Structure of a Transmembrane Region and a Cytoplasmic Loop of the Human Red Cell Anion Exchanger (Band3, AE1)
Authors: Chambers, E.J. / Bloomberg, G.B. / Ring, S.M. / Tanner, M.J.A.
History
DepositionNov 1, 1998Deposition site: PDBE / Processing site: RCSB
Revision 1.0Jun 1, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (BAND 3 ANION TRANSPORT PROTEIN)


Theoretical massNumber of molelcules
Total (without water)4,6281
Polymers4,6281
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)21 / 50NO NOE VIOLATIONS GREATER THAN 0.05 NM, NO DIHEDRAL VIOLATIONS GREATER THAN 5 DEGREES.
RepresentativeModel #8

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Components

#1: Protein/peptide PROTEIN (BAND 3 ANION TRANSPORT PROTEIN)


Mass: 4628.324 Da / Num. of mol.: 1 / Fragment: C-TERMINAL CYTOPLASM/FIRST MEMBRANE SPAN / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING FMOC PEPTIDE STRATEGY. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN THE CYTOPLASM/MEMBRANE RED CELL OF HOMO SAPIENS.
References: UniProt: P02730

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
131HOHAHA
1412D HSQC
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR AND 2D N-15/H-1 HETERONUCLEAR NMR SPECTROSCOPY.

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Sample preparation

Sample conditionspH: 3.5 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: JEOL ALPHA 500 / Manufacturer: JEOL / Model: ALPHA 500 / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE EUR. J. BIOCHEM. 1994, V221, 445-454.
NMR ensembleConformer selection criteria: NO NOE VIOLATIONS GREATER THAN 0.05 NM, NO DIHEDRAL VIOLATIONS GREATER THAN 5 DEGREES.
Conformers calculated total number: 50 / Conformers submitted total number: 21

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