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Solution structure of Copper-CopAS46V from Bacillus subtilis
Authors
Banci, L., Bertini, I., Ciofi-Baffoni, S., Gonnelli, L., Su, X.C.
Assembly
Potential copper-transporting ATPase
Entity
1. CPx-type ATPase CopA (polymer, Thiol state: all other bound), 76 monomers, 8165.353 Da Detail

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVIEGR


2. CU1 (non-polymer), 63.546 Da
Total weight
8228.899 Da
Max. entity weight
8165.353 Da
Entity Connection
na 2 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1nasing1:CYS17:SG2:CU11:CU
2nasing1:CYS20:SG2:CU11:CU

Source organism
Bacillus subtilis
Exptl. method
NMR
Refine. method
distance geometry,
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.1 %, Completeness: 88.3 %, Completeness (bb): 95.7 % Detail

Polymer type: polypeptide(L)

Total1H15N
All88.3 % (452 of 512)86.8 % (375 of 432)96.2 % (77 of 80)
Backbone95.7 % (220 of 230)95.5 % (149 of 156)95.9 % (71 of 74)
Sidechain82.3 % (232 of 282)81.9 % (226 of 276)100.0 % (6 of 6)
Aromatic40.0 % (4 of 10)40.0 % (4 of 10)
Methyl94.0 % (47 of 50)94.0 % (47 of 50)

1. CPx-type ATPase CopA

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVIEGR

Sample

Pressure 1 atm, Temperature 298 (±0.1) K, pH 7.0 (±0.1)


#NameIsotope labelingTypeConcentration
1CPx-type ATPase CopA[U-15N]1.2 mM
2phosphate20 mM
3H2O90 %
4D2O10 %

Protein Blocks Logo
Calculated from 30 models in PDB: 1OQ6, Strand ID: A Detail


Release date
2003-09-07
Citation
A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis
Banci, L., Bertini, I., Ciofi-Baffoni, S., Gonnelli, L., Su, X.C.
J. Mol. Biol. (2003), 331, 473-484, PubMed 12888353 , DOI: ,
Related entities 1. CPx-type ATPase CopA, : 1 : 2 : 2 : 285 entities Detail
Interaction partners 1. CPx-type ATPase CopA, : 2 interactors Detail
Experiments performed 5 experiments Detail
nullKeywords CopA, copper protein, folding, mutation, NMR, P-type ATPase