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Calcium in PDB 8fna: Crystal Structure of the C-Terminal Fg Domain of Human Tnr

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Fg Domain of Human Tnr, PDB code: 8fna was solved by S.Bouyain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.08 / 1.75
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 47.423, 47.423, 203.403, 90, 90, 120
R / Rfree (%) 16 / 18.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the C-Terminal Fg Domain of Human Tnr (pdb code 8fna). 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 Crystal Structure of the C-Terminal Fg Domain of Human Tnr, PDB code: 8fna:

Calcium binding site 1 out of 1 in 8fna

Go back to Calcium Binding Sites List in 8fna
Calcium binding site 1 out of 1 in the Crystal Structure of the C-Terminal Fg Domain of Human Tnr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the C-Terminal Fg Domain of Human Tnr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1401

b:25.9
occ:1.00
OD1 A:ASP1284 2.2 25.5 1.0
O A:THR1288 2.3 27.8 1.0
O A:HOH1551 2.4 27.9 1.0
OD2 A:ASP1282 2.4 25.0 1.0
O A:HOH1665 2.4 30.0 1.0
O A:ALA1286 2.5 30.4 1.0
OD1 A:ASP1282 2.7 28.5 1.0
CG A:ASP1282 2.9 29.2 1.0
CG A:ASP1284 3.1 22.7 1.0
OD2 A:ASP1284 3.4 24.6 1.0
HA A:ASN1289 3.5 27.3 1.0
C A:THR1288 3.5 28.1 1.0
C A:ALA1286 3.6 32.6 1.0
H A:ALA1286 3.6 31.1 1.0
HB3 A:ALA1286 3.7 31.8 1.0
H A:ASP1284 4.1 27.0 1.0
N A:ALA1286 4.1 25.9 1.0
O A:ASP1284 4.2 27.6 1.0
O A:HOH1687 4.2 41.7 1.0
C A:VAL1287 4.2 33.7 1.0
CA A:ALA1286 4.2 27.1 1.0
N A:ASN1289 4.3 23.9 1.0
H A:CYS1290 4.3 22.6 1.0
CA A:ASN1289 4.3 22.7 1.0
O A:VAL1287 4.3 42.1 1.0
C A:ASP1284 4.3 23.9 1.0
N A:THR1288 4.4 35.4 1.0
CB A:ASP1282 4.4 29.2 1.0
O A:HOH1544 4.4 36.5 1.0
HA A:VAL1287 4.4 41.3 1.0
CB A:ASP1284 4.4 23.3 1.0
CB A:ALA1286 4.4 26.5 1.0
O A:HOH1526 4.5 30.4 1.0
CA A:THR1288 4.5 35.2 1.0
N A:VAL1287 4.6 33.1 1.0
N A:ASP1284 4.6 22.5 1.0
CA A:VAL1287 4.7 34.4 1.0
HB3 A:ASP1282 4.7 35.1 1.0
H A:THR1288 4.7 42.5 1.0
CA A:ASP1284 4.7 22.9 1.0
HB2 A:ASP1282 4.8 35.1 1.0
N A:VAL1285 4.9 26.5 1.0
HB2 A:ASP1284 4.9 28.0 1.0
N A:CYS1290 4.9 18.8 1.0
HB1 A:ALA1286 4.9 31.8 1.0
HA A:THR1288 5.0 42.3 1.0
HB2 A:ASN1289 5.0 28.1 1.0
HA A:VAL1285 5.0 32.5 1.0

Reference:

A.Sinha, J.Kawakami, K.S.Cole, A.Ladutska, M.Y.Nguyen, M.S.Zalmai, B.L.Holder, V.M.Broerman, R.T.Matthews, S.Bouyain. Protein-Protein Interactions Between Tenascin-R and Rptp Zeta /Phosphacan Are Critical to Maintain the Architecture of Perineuronal Nets. J.Biol.Chem. 04952 2023.
ISSN: ESSN 1083-351X
PubMed: 37356715
DOI: 10.1016/J.JBC.2023.104952
Page generated: Fri Jul 19 09:01:49 2024

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