Search

Solution structure of apoCadA
Authors
Banci, L., Bertini, I., Ciofi-Baffoni, S., Su, X., Miras, R., Bal, N., Mintz, E., Catty, P., Shokes, J.E., Scott, R.A.
Assembly
cadmium-transporting ATPase (E.C.3.6.3.3)
Entity
1. cadmium-transporting ATPase (E.C.3.6.3.3) (polymer, Thiol state: all free), 71 monomers, 7699.653 Da Detail

MAEKTVYRVD GLSCTNCAAK FERNVKEIEG VTEAIVNFGA SKITVTGEAS IQQVEQAGAF EHLKIIPEKE A


Formula weight
7699.653 Da
Source organism
Listeria monocytogenes
Exptl. method
NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.6 %, Completeness: 93.0 %, Completeness (bb): 97.7 % Detail

Polymer type: polypeptide(L)

Total1H15N
All93.0 % (454 of 488)92.2 % (380 of 412)97.4 % (74 of 76)
Backbone97.7 % (211 of 216)97.9 % (143 of 146)97.1 % (68 of 70)
Sidechain89.3 % (243 of 272)89.1 % (237 of 266)100.0 % (6 of 6)
Aromatic90.5 % (19 of 21)90.5 % (19 of 21)
Methyl97.7 % (43 of 44)97.7 % (43 of 44)

1. P-type ATPase

MAEKTVYRVD GLSCTNCAAK FERNVKEIEG VTEAIVNFGA SKITVTGEAS IQQVEQAGAF EHLKIIPEKE A

Sample

Pressure 1 atm, Temperature 298 (±1) K, pH 7.0 (±0.2)


#NameIsotope labelingTypeConcentration
1P-type ATPase[U-15N]2 mM
2sodium phosphate buffer350 mM
3TCEP5 mM
4H2O90 %
5D2O10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2AJ0, Strand ID: A Detail


Release date
2007-01-25
Citation
Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA
Banci, L., Bertini, I., Ciofi-Baffoni, S., Su, X., Miras, R., Bal, N., Mintz, E., Catty, P., Shokes, J.E., Scott, R.A.
J. Mol. Biol. (2006), 356, 638-650, PubMed 16388822 , DOI 10.1016/j.jmb.2005.11.055 ,
Related entities 1. cadmium-transporting ATPase (E.C.3.6.3.3), : 1 : 1 : 1 : 50 entities Detail
Experiments performed 5 experiments Detail
nullKeywords beta-alpha-beta-beta-alpha-beta, ferrodoxin-like fold, metal binding protein