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Second Metal Binding Domain of the Menkes ATPase
Authors
Jones, C.E., Daly, N.L., Cobine, P.A., Craik, D.J., Dameron, C.T.
Assembly
Copper-transporting ATPase 1
Entity
1. Copper-transporting ATPase 1 (polymer, Thiol state: all free), 84 monomers, 9294.894 Da Detail

GSMAQAGEVV LKMKVEGMTC HSCTSTIEGK IGKLQGVQRI KVSLDNQEAT IVYQPHLISV EEMKKQIEAM GFPAFVKKQP KYLK


Formula weight
9294.894 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
Molecular dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 92.9 %, Completeness: 81.6 %, Completeness (bb): 89.3 % Detail

Polymer type: polypeptide(L)

Total1H15N
All81.6 % (502 of 615)81.6 % (429 of 526)82.0 % (73 of 89)
Backbone89.3 % (226 of 253)90.1 % (155 of 172)87.7 % (71 of 81)
Sidechain76.2 % (276 of 362)77.4 % (274 of 354)25.0 % (2 of 8)
Aromatic68.2 % (15 of 22)68.2 % (15 of 22)
Methyl93.6 % (44 of 47)93.6 % (44 of 47)

1. Menkes ATPase subdomain2

GSMAQAGEVV LKMKVEGMTC HSCTSTIEGK IGKLQGVQRI KVSLDNQEAT IVYQPHLISV EEMKKQIEAM GFPAFVKKQP KYLK

Sample

Pressure 1 atm, Temperature 298 (±1) K, pH 6.5 (±0.2)


#NameIsotope labelingTypeConcentration
1Menkes ATPase subdomain2[U-15N]0.5 mM
2potassium phosphate20 mM
3sodium chloride10 mM
4H2O90 %
5D2O10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 1Q8L, Strand ID: A Detail


Release date
2004-02-12
Citation
Structure and metal binding studies of the second copper binding domain of the Menkes ATPase
Jones, C.E., Daly, N.L., Cobine, P.A., Craik, D.J., Dameron, C.T.
J. Struct. Biol. (2003), 143, 209-218, PubMed 14572476 , DOI: ,
Related entities 1. Copper-transporting ATPase 1, : 1 : 4 : 138 entities Detail
Interaction partners 1. Copper-transporting ATPase 1, : 5 interactors Detail
Experiments performed 5 experiments Detail
nullKeywords METAL BINDING PROTEIN