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- PDB-1h7d: Solution structure of the 49 aa presequence of 5-ALAS -

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Basic information

Entry
Database: PDB / ID: 1h7d
TitleSolution structure of the 49 aa presequence of 5-ALAS
ComponentsAMINOLEVULINIC ACID SYNTHASE 2, ERYTHROID
KeywordsACYLTRANSFERASE / ALAS / PRESEQUENCE
Function / homology
Function and homology information


Heme biosynthesis / 5-aminolevulinate synthase / 5-aminolevulinate synthase activity / hemoglobin biosynthetic process / coenzyme A binding / protoporphyrinogen IX biosynthetic process / heme biosynthetic process / erythrocyte development / erythrocyte differentiation / pyridoxal phosphate binding ...Heme biosynthesis / 5-aminolevulinate synthase / 5-aminolevulinate synthase activity / hemoglobin biosynthetic process / coenzyme A binding / protoporphyrinogen IX biosynthetic process / heme biosynthetic process / erythrocyte development / erythrocyte differentiation / pyridoxal phosphate binding / intracellular iron ion homeostasis / mitochondrial inner membrane / response to hypoxia / mitochondrial matrix / mitochondrion
Similarity search - Function
Aminolevulinic Acid Synthase 2 / Aminolevulinic Acid Synthase 2 / 5-aminolevulinate synthase presequence / 5-aminolevulinate synthase presequence / Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase / Aminotransferase, class-II, pyridoxal-phosphate binding site / Aminotransferases class-II pyridoxal-phosphate attachment site. / Aminotransferase, class I/classII / Aminotransferase class I and II / Pyridoxal phosphate-dependent transferase, small domain ...Aminolevulinic Acid Synthase 2 / Aminolevulinic Acid Synthase 2 / 5-aminolevulinate synthase presequence / 5-aminolevulinate synthase presequence / Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase / Aminotransferase, class-II, pyridoxal-phosphate binding site / Aminotransferases class-II pyridoxal-phosphate attachment site. / Aminotransferase, class I/classII / Aminotransferase class I and II / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Few Secondary Structures / Irregular
Similarity search - Domain/homology
5-aminolevulinate synthase, erythroid-specific, mitochondrial / 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsGoodfellow, B.J. / Dias, J.S. / Ferreira, G.C. / Wray, V. / Henklein, P. / Macedo, A.L.
CitationJournal: FEBS Lett. / Year: 2001
Title: The Solution Structure and Heme Binding of the Presequence of Murine 5-Aminolevulinate Synthase
Authors: Goodfellow, B.J. / Dias, J.S. / Ferreira, G.C. / Henklein, P. / Wray, V. / Macedo, A.L.
History
DepositionJul 5, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 18, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: AMINOLEVULINIC ACID SYNTHASE 2, ERYTHROID


Theoretical massNumber of molelcules
Total (without water)5,1021
Polymers5,1021
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 30LOW TARGET FUNCTION
RepresentativeModel #21

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Components

#1: Protein/peptide AMINOLEVULINIC ACID SYNTHASE 2, ERYTHROID / AMINO LEVULINATE SYNTHASE / 5-AMINOLEVULINIC ACID SYNTHASE / DELTA-AMINOLEVULINATE SYNTHASE / DELTA- ...AMINO LEVULINATE SYNTHASE / 5-AMINOLEVULINIC ACID SYNTHASE / DELTA-AMINOLEVULINATE SYNTHASE / DELTA-ALA SYNTHETASE


Mass: 5102.136 Da / Num. of mol.: 1 / Fragment: PRESEQUENCE RESIDUES 1-49 / Source method: obtained synthetically / Source: (synth.) MUS MUSCULUS (house mouse)
References: UniProt: Q64452, UniProt: P08680*PLUS, 5-aminolevulinate synthase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
131TOCSY
NMR detailsText: 150MS NOESY, 70MS TOCSY

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Sample preparation

Sample conditionspH: 5 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
DYANAGUNTERT,WUTHRICHrefinement
DYANAstructure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: LOW TARGET FUNCTION / Conformers calculated total number: 30 / Conformers submitted total number: 30

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