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- PDB-1aoo: AG-SUBSTITUTED METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR... -

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Basic information

Entry
Database: PDB / ID: 1aoo
TitleAG-SUBSTITUTED METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsAG-METALLOTHIONEIN
KeywordsMETALLOTHIONEIN / COPPER DETOXIFICATION / METAL-THIOLATE CLUSTER
Function / homology
Function and homology information


detoxification of cadmium ion / detoxification of copper ion / response to copper ion / cadmium ion binding / superoxide dismutase activity / antioxidant activity / removal of superoxide radicals / copper ion binding / cytosol
Similarity search - Function
Ag-metallothionein / Metallothionein domain superfamily, yeast / Metallothionein domain, yeast / Copper metallothionein superfamily / Yeast metallothionein / Metallothionein domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
SILVER ION / Copper metallothionein 1-1 / Copper metallothionein 1-1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / distance geometry
AuthorsPeterson, C.W. / Narula, S.S. / Armitage, I.M.
CitationJournal: FEBS Lett. / Year: 1996
Title: 3D solution structure of copper and silver-substituted yeast metallothioneins.
Authors: Peterson, C.W. / Narula, S.S. / Armitage, I.M.
History
DepositionJul 8, 1997Processing site: BNL
Revision 1.0Dec 24, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 22, 2024Group: 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: AG-METALLOTHIONEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)5,0318
Polymers4,2761
Non-polymers7557
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 30LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide AG-METALLOTHIONEIN / AG-MT


Mass: 4275.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: AG(I) SUBSTITUTED / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: 301N / References: UniProt: P07215, UniProt: P0CX80*PLUS
#2: Chemical
ChemComp-AG / SILVER ION


Mass: 107.868 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Ag

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111COSY
121AG-FILTERED COSY
131RELAY-COSY
141TOCSY
151NOESY
1611H-109AG HMQC

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 283 K

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NMR measurement

NMR spectrometerType: Bruker AM 500 / Manufacturer: Bruker / Model: AM 500 / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 30 / Conformers submitted total number: 1

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