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Calcium in PDB 2w2p: PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr

Protein crystallography data

The structure of PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr, PDB code: 2w2p was solved by M.J.Bottomley, A.Cirillo, L.Orsatti, L.Ruggeri, T.S.Fisher, J.C.Santoro, R.T.Cummings, R.M.Cubbon, P.Lo Surdo, A.Calzetta, A.Noto, J.Baysarowich, M.Mattu, F.Talamo, R.De Francesco, C.P.Sparrow, A.Sitlani, A.Carfi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.62
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 84.106, 84.106, 209.745, 90.00, 90.00, 90.00
R / Rfree (%) 22.589 / 27.02

Calcium Binding Sites:

The binding sites of Calcium atom in the PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr (pdb code 2w2p). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr, PDB code: 2w2p:

Calcium binding site 1 out of 1 in 2w2p

Go back to Calcium Binding Sites List in 2w2p
Calcium binding site 1 out of 1 in the PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of PCSK9-Deltac D374A Mutant Bound to Wt Egf-A of Ldlr within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca1333

b:46.9
occ:1.00
OD2 E:ASP310 2.4 31.9 1.0
O E:GLY314 2.4 35.9 1.0
O E:THR294 2.5 32.6 1.0
O E:LEU311 2.5 34.0 1.0
OE1 E:GLU296 2.5 35.2 1.0
CD E:GLU296 3.4 35.0 1.0
C E:GLY314 3.5 36.3 1.0
CG E:ASP310 3.5 31.4 1.0
OE2 E:GLU296 3.6 34.9 1.0
C E:LEU311 3.6 34.0 1.0
C E:THR294 3.7 32.6 1.0
N E:LEU311 3.9 33.2 1.0
N E:GLY314 3.9 35.6 1.0
CA E:GLY314 4.1 35.9 1.0
OD1 E:ASP310 4.1 31.1 1.0
C E:ASP310 4.2 32.8 1.0
O E:LYS312 4.2 35.0 1.0
N E:THR294 4.3 32.6 1.0
CA E:LEU311 4.3 33.7 1.0
CA E:ASP310 4.4 32.5 1.0
C E:LYS312 4.5 34.9 1.0
CA E:ASN295 4.5 32.4 1.0
N E:ASN295 4.5 32.4 1.0
C E:ILE313 4.5 35.4 1.0
CB E:ASP310 4.6 32.3 1.0
N E:GLU296 4.6 32.9 1.0
CA E:THR294 4.6 32.7 1.0
N E:TYR315 4.6 36.7 1.0
N E:LYS312 4.7 34.4 1.0
CB E:TYR315 4.8 37.1 1.0
O E:ALA291 4.8 31.4 1.0
O E:ASP310 4.8 32.9 1.0
CG E:GLU296 4.9 34.1 1.0
N E:ILE313 5.0 35.1 1.0
CA E:LYS312 5.0 34.8 1.0

Reference:

M.J.Bottomley, A.Cirillo, L.Orsatti, L.Ruggeri, T.S.Fisher, J.C.Santoro, R.T.Cummings, R.M.Cubbon, P.Lo Surdo, A.Calzetta, A.Noto, J.Baysarowich, M.Mattu, F.Talamo, R.De Francesco, C.P.Sparrow, A.Sitlani, A.Carfi. Structural and Biochemical Characterization of the Wild Type PCSK9/Egf-Ab Complex and Natural Fh Mutants. J.Biol.Chem. V. 284 1313 2009.
ISSN: ISSN 0021-9258
PubMed: 19001363
DOI: 10.1074/JBC.M808363200
Page generated: Fri Jul 12 18:26:29 2024

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