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Zinc in PDB 4m3o: Crystal Structure of K.Lactis RTR1 Ntd

Protein crystallography data

The structure of Crystal Structure of K.Lactis RTR1 Ntd, PDB code: 4m3o was solved by P.L.Hsu, W.Yang, N.Zheng, G.Varani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.44 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.272, 88.920, 102.488, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of K.Lactis RTR1 Ntd (pdb code 4m3o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of K.Lactis RTR1 Ntd, PDB code: 4m3o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4m3o

Go back to Zinc Binding Sites List in 4m3o
Zinc binding site 1 out of 2 in the Crystal Structure of K.Lactis RTR1 Ntd


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of K.Lactis RTR1 Ntd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:39.8
occ:1.00
ND1 A:HIS115 2.2 41.1 1.0
SG A:CYS111 2.3 42.3 1.0
SG A:CYS78 2.3 36.8 1.0
SG A:CYS73 2.3 35.4 1.0
CB A:CYS73 3.1 36.0 1.0
CB A:CYS78 3.1 39.6 1.0
CE1 A:HIS115 3.2 44.4 1.0
CG A:HIS115 3.2 39.2 1.0
CB A:CYS111 3.4 41.0 1.0
CB A:HIS115 3.6 36.2 1.0
N A:CYS111 3.9 42.1 1.0
CA A:CYS111 4.3 43.6 1.0
NE2 A:HIS115 4.3 43.0 1.0
CD2 A:HIS115 4.4 43.5 1.0
CA A:CYS73 4.5 37.8 1.0
CA A:CYS78 4.6 41.7 1.0
CB A:TYR75 4.8 34.8 1.0
CB A:LYS80 4.9 46.7 1.0
OG1 A:THR112 5.0 37.8 1.0

Zinc binding site 2 out of 2 in 4m3o

Go back to Zinc Binding Sites List in 4m3o
Zinc binding site 2 out of 2 in the Crystal Structure of K.Lactis RTR1 Ntd


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of K.Lactis RTR1 Ntd within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn300

b:29.2
occ:1.00
ND1 B:HIS115 2.1 31.1 1.0
SG B:CYS73 2.3 27.1 1.0
SG B:CYS78 2.3 31.3 1.0
SG B:CYS111 2.3 30.2 1.0
CE1 B:HIS115 3.0 36.4 1.0
CB B:CYS78 3.1 31.0 1.0
CB B:CYS73 3.1 28.2 1.0
CG B:HIS115 3.2 28.4 1.0
CB B:CYS111 3.4 31.3 1.0
CB B:HIS115 3.6 28.4 1.0
N B:CYS111 3.9 29.7 1.0
NE2 B:HIS115 4.1 35.7 1.0
CD2 B:HIS115 4.3 33.4 1.0
CA B:CYS111 4.3 30.3 1.0
CA B:CYS78 4.5 39.5 1.0
CA B:CYS73 4.6 27.8 1.0
OG1 B:THR112 4.8 28.4 1.0
CB B:TYR75 4.9 28.7 1.0
N B:THR112 4.9 27.8 1.0
CB B:LYS80 4.9 34.7 1.0

Reference:

P.L.Hsu, F.Yang, W.Smith-Kinnaman, W.Yang, J.E.Song, A.L.Mosley, G.Varani. RTR1 Is A Dual Specificity Phosphatase That Dephosphorylates TYR1 and SER5 on the Rna Polymerase II Ctd. J.Mol.Biol. V. 426 2970 2014.
ISSN: ISSN 0022-2836
PubMed: 24951832
DOI: 10.1016/J.JMB.2014.06.010
Page generated: Sun Oct 27 02:16:27 2024

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