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Chlorine in PDB 5ntu: Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution

Protein crystallography data

The structure of Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution, PDB code: 5ntu was solved by T.R.Cotton, G.Fischer, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.27 / 2.58
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 168.157, 36.301, 120.448, 90.00, 104.39, 90.00
R / Rfree (%) 21.5 / 26

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution (pdb code 5ntu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution, PDB code: 5ntu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5ntu

Go back to Chlorine Binding Sites List in 5ntu
Chlorine binding site 1 out of 2 in the Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:0.4
occ:1.00
NZ A:LYS209 3.1 79.2 1.0
O A:VAL151 3.5 70.1 1.0
NE2 A:GLN213 3.5 65.7 1.0
CE A:LYS209 3.6 67.6 1.0
O A:ASN149 4.5 86.5 1.0
CD A:GLN213 4.5 77.7 1.0
OE1 A:GLN213 4.6 72.4 1.0
C A:VAL151 4.7 69.0 1.0

Chlorine binding site 2 out of 2 in 5ntu

Go back to Chlorine Binding Sites List in 5ntu
Chlorine binding site 2 out of 2 in the Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Pro-Myostatin Precursor at 2.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl401

b:97.9
occ:1.00
N B:ASP289 3.4 57.5 1.0
CE1 B:PHE293 3.6 67.2 1.0
C1 B:EDO410 3.6 99.7 1.0
O B:THR287 3.7 61.2 1.0
CA B:VAL288 4.0 56.5 1.0
CZ B:PHE293 4.1 64.9 1.0
C B:VAL288 4.2 59.7 1.0
CB B:ASP289 4.2 60.6 1.0
O B:ASP289 4.2 60.5 1.0
CA B:ASP289 4.3 57.5 1.0
C2 B:EDO410 4.5 97.0 1.0
CD1 B:PHE293 4.6 67.3 1.0
C B:THR287 4.6 60.3 1.0
C B:ASP289 4.7 59.7 1.0
O1 B:EDO410 4.8 0.4 1.0
CB B:ALA292 4.8 64.0 1.0
N B:VAL288 4.8 57.1 1.0
CB B:VAL288 4.9 60.7 1.0
CG2 B:ILE53 5.0 60.3 1.0
CG1 B:VAL288 5.0 59.8 1.0

Reference:

T.R.Cotton, G.Fischer, X.Wang, J.C.Mccoy, M.Czepnik, T.B.Thompson, M.Hyvonen. Structure of the Human Myostatin Precursor and Determinants of Growth Factor Latency. Embo J. V. 37 367 2018.
ISSN: ESSN 1460-2075
PubMed: 29330193
DOI: 10.15252/EMBJ.201797883
Page generated: Sat Dec 12 12:10:34 2020

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