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Calcium in PDB 1tvg: X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958.

Protein crystallography data

The structure of X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958., PDB code: 1tvg was solved by A.P.Kuzin, S.M.Vorobiev, I.Lee, T.B.Acton, G.T.Montelione, L.Tong, J.F.Hunt, Northeast Structural Genomics Consortium(Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.74 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.974, 41.617, 46.779, 90.00, 102.19, 90.00
R / Rfree (%) 21.5 / 24.4

Other elements in 1tvg:

The structure of X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958. also contains other interesting chemical elements:

Samarium (Sm) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958. (pdb code 1tvg). 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 X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958., PDB code: 1tvg:

Calcium binding site 1 out of 1 in 1tvg

Go back to Calcium Binding Sites List in 1tvg
Calcium binding site 1 out of 1 in the X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of X-Ray Structure of Human PP25 Gene Product, HSPC034. Northeast Structural Genomics Target HR1958. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca221

b:6.0
occ:1.00
O A:ASN29 2.4 8.1 1.0
O A:ASN34 2.5 11.5 1.0
O A:HIS130 2.6 6.9 1.0
O A:THR37 2.6 7.5 1.0
O A:HOH334 2.6 8.1 1.0
OD1 A:ASP32 2.6 10.4 1.0
OG1 A:THR37 2.6 8.0 1.0
C A:THR37 3.5 9.1 1.0
C A:ASN34 3.5 12.4 1.0
C A:ASN29 3.6 8.2 1.0
CG A:ASP32 3.7 12.8 1.0
C A:HIS130 3.7 6.6 1.0
CB A:THR37 3.8 9.5 1.0
OD2 A:ASP32 4.0 14.4 1.0
N A:ASN34 4.0 13.6 1.0
CA A:THR37 4.0 8.6 1.0
N A:THR37 4.1 10.9 1.0
CA A:ASN34 4.2 12.3 1.0
CB A:ASN34 4.3 13.1 1.0
CA A:ASN29 4.3 9.5 1.0
CA A:HIS130 4.5 6.1 1.0
N A:PHE38 4.5 8.0 1.0
N A:ILE30 4.6 6.4 1.0
CB A:ASN29 4.6 9.2 1.0
N A:PRO35 4.6 13.0 1.0
CA A:ILE30 4.7 7.1 1.0
N A:ASP32 4.7 10.7 1.0
C A:ILE30 4.7 8.2 1.0
N A:SER131 4.7 7.3 1.0
CA A:PHE38 4.8 8.7 1.0
CA A:PRO35 4.8 12.3 1.0
C A:PRO35 4.8 12.8 1.0
CB A:SER131 4.8 10.0 1.0
O A:ILE30 4.8 7.2 1.0
CA A:SER131 4.9 7.9 1.0
N A:GLY33 4.9 11.2 1.0
CG2 A:THR37 5.0 10.2 1.0
CB A:ASP32 5.0 12.3 1.0

Reference:

T.A.Ramelot, S.Raman, A.P.Kuzin, R.Xiao, L.C.Ma, T.B.Acton, J.F.Hunt, G.T.Montelione, D.Baker, M.A.Kennedy. Improving uc(Nmr) Protein Structure Quality By Rosetta Refinement: A Molecular Replacement Study. Proteins V. 75 147 2009.
ISSN: ISSN 0887-3585
PubMed: 18816799
DOI: 10.1002/PROT.22229
Page generated: Tue Jul 8 02:21:56 2025

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