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Zinc in PDB 5w0b: Structure of Human TUT7 Catalytic Module (Cm)

Enzymatic activity of Structure of Human TUT7 Catalytic Module (Cm)

All present enzymatic activity of Structure of Human TUT7 Catalytic Module (Cm):
2.7.7.52;

Protein crystallography data

The structure of Structure of Human TUT7 Catalytic Module (Cm), PDB code: 5w0b was solved by C.R.Faehnle, J.Walleshauser, L.Joshua-Tor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.16 / 2.61
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 141.232, 141.232, 174.475, 90.00, 90.00, 120.00
R / Rfree (%) 23.1 / 25.5

Other elements in 5w0b:

The structure of Structure of Human TUT7 Catalytic Module (Cm) also contains other interesting chemical elements:

Iodine (I) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human TUT7 Catalytic Module (Cm) (pdb code 5w0b). 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 Structure of Human TUT7 Catalytic Module (Cm), PDB code: 5w0b:

Zinc binding site 1 out of 1 in 5w0b

Go back to Zinc Binding Sites List in 5w0b
Zinc binding site 1 out of 1 in the Structure of Human TUT7 Catalytic Module (Cm)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human TUT7 Catalytic Module (Cm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1401

b:0.2
occ:1.00
HG A:CYS1347 1.6 0.6 1.0
NE2 A:HIS1355 2.1 0.9 1.0
HG A:CYS1350 2.3 0.7 1.0
SG A:CYS1350 2.4 0.4 1.0
SG A:CYS1360 2.4 0.9 1.0
SG A:CYS1347 2.5 0.5 1.0
HB3 A:CYS1347 2.5 0.3 1.0
HB3 A:CYS1350 2.6 0.6 1.0
HB2 A:CYS1347 2.7 0.3 1.0
CB A:CYS1347 2.7 0.9 1.0
HB2 A:CYS1360 2.8 0.2 1.0
CD2 A:HIS1355 3.0 0.3 1.0
CB A:CYS1350 3.0 0.4 1.0
CE1 A:HIS1355 3.0 0.5 1.0
H A:CYS1350 3.1 0.4 1.0
CB A:CYS1360 3.1 0.2 1.0
HD2 A:HIS1355 3.2 0.2 1.0
HE1 A:HIS1355 3.2 0.2 1.0
HG23 A:ILE1349 3.4 0.6 1.0
HG A:CYS1360 3.5 0.9 1.0
HB2 A:CYS1350 3.7 0.6 1.0
HB3 A:CYS1360 3.7 0.2 1.0
N A:CYS1350 3.8 0.5 1.0
CA A:CYS1350 4.0 0.2 1.0
ND1 A:HIS1355 4.1 0.0 1.0
CG A:HIS1355 4.1 0.8 1.0
HA A:CYS1360 4.1 0.9 1.0
H A:LYS1352 4.2 0.7 1.0
CA A:CYS1347 4.2 0.8 1.0
CA A:CYS1360 4.3 0.1 1.0
CG2 A:ILE1349 4.3 0.0 1.0
H A:GLY1351 4.3 0.8 1.0
HG13 A:ILE1349 4.4 0.1 1.0
HD2 A:PRO1361 4.5 0.8 1.0
HG21 A:ILE1349 4.6 0.6 1.0
HB2 A:LYS1352 4.6 0.2 1.0
H A:ILE1349 4.6 0.2 1.0
H A:CYS1347 4.6 0.9 1.0
O A:LYS1352 4.6 0.2 1.0
HA A:CYS1347 4.7 0.5 1.0
O A:PHE1356 4.7 0.4 1.0
HA A:CYS1350 4.7 0.1 1.0
HG22 A:ILE1349 4.8 0.6 1.0
N A:GLY1351 4.8 0.9 1.0
HA A:MET1357 4.8 0.2 1.0
C A:CYS1350 4.8 0.9 1.0
HD1 A:HIS1355 4.9 0.8 1.0
C A:CYS1347 4.9 0.3 1.0
N A:CYS1347 5.0 0.6 1.0
C A:ILE1349 5.0 0.4 1.0

Reference:

C.R.Faehnle, J.Walleshauser, L.Joshua-Tor. Multi-Domain Utilization By TUT4 and TUT7 in Control of Let-7 Biogenesis. Nat. Struct. Mol. Biol. V. 24 658 2017.
ISSN: ESSN 1545-9985
PubMed: 28671666
DOI: 10.1038/NSMB.3428
Page generated: Wed Dec 16 11:13:44 2020

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