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Zinc in PDB 4dgw: Crystal Structure of the SF3A Splicing Factor Complex of U2 Snrnp

Protein crystallography data

The structure of Crystal Structure of the SF3A Splicing Factor Complex of U2 Snrnp, PDB code: 4dgw was solved by P.C.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.86 / 3.11
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.781, 127.259, 169.173, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 27.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the SF3A Splicing Factor Complex of U2 Snrnp (pdb code 4dgw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the SF3A Splicing Factor Complex of U2 Snrnp, PDB code: 4dgw:

Zinc binding site 1 out of 1 in 4dgw

Go back to Zinc Binding Sites List in 4dgw
Zinc binding site 1 out of 1 in the Crystal Structure of the SF3A Splicing Factor Complex of U2 Snrnp


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 the SF3A Splicing Factor Complex of U2 Snrnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:0.9
occ:1.00
NE2 A:HIS298 2.4 0.2 1.0
ND1 A:HIS304 2.4 1.0 1.0
SG A:CYS282 2.5 0.7 1.0
SG A:CYS285 2.7 1.0 1.0
CE1 A:HIS298 3.1 0.8 1.0
CG A:HIS304 3.2 0.0 1.0
CB A:CYS285 3.2 0.1 1.0
CE1 A:HIS304 3.3 0.6 1.0
CD2 A:HIS298 3.5 0.7 1.0
CB A:HIS304 3.5 0.1 1.0
CB A:CYS282 3.6 0.9 1.0
N A:CYS285 3.9 96.2 1.0
CA A:CYS285 4.2 99.9 1.0
CA A:HIS304 4.2 1.0 1.0
ND1 A:HIS298 4.3 0.6 1.0
NE2 A:HIS304 4.3 0.5 1.0
CD2 A:HIS304 4.3 0.3 1.0
CB A:PHE284 4.4 89.9 1.0
CG A:HIS298 4.5 0.6 1.0
CD2 A:LEU299 4.5 0.6 1.0
C A:PHE284 4.6 95.0 1.0
CZ A:PHE289 4.9 0.5 1.0
CA A:PHE284 4.9 93.1 1.0
CE2 A:PHE289 5.0 0.6 1.0

Reference:

P.C.Lin, R.M.Xu. Structure and Assembly of the SF3A Splicing Factor Complex of U2 Snrnp Embo J. V. 31 1579 2012.
ISSN: ISSN 0261-4189
PubMed: 22314233
DOI: 10.1038/EMBOJ.2012.7
Page generated: Sat Oct 26 21:26:30 2024

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