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Zinc in PDB 6zxh: Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2

Enzymatic activity of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2

All present enzymatic activity of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2:
2.7.11.1; 4.2.99.18;

Other elements in 6zxh:

The structure of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2 also contains other interesting chemical elements:

Magnesium (Mg) 131 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2 (pdb code 6zxh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2, PDB code: 6zxh:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 6zxh

Go back to Zinc Binding Sites List in 6zxh
Zinc binding site 1 out of 3 in the Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
h:Zn201

b:28.4
occ:1.00
SG h:CYS26 2.4 6.8 1.0
SG h:CYS74 2.4 5.8 1.0
SG h:CYS77 2.5 6.4 1.0
SG h:CYS23 2.5 5.8 1.0
CB h:CYS23 3.2 5.8 1.0
CB h:CYS26 3.3 6.8 1.0
CB h:CYS77 3.5 6.4 1.0
CB h:CYS74 3.6 5.8 1.0
N h:CYS26 3.7 6.8 1.0
CA h:CYS26 4.1 6.8 1.0
N h:CYS74 4.2 5.8 1.0
CA h:CYS74 4.5 5.8 1.0
CB h:ARG28 4.5 5.8 1.0
CB h:ASN25 4.5 7.1 1.0
N h:CYS77 4.5 6.4 1.0
ND2 h:ASN25 4.6 7.1 1.0
CA h:CYS77 4.6 6.4 1.0
C h:CYS26 4.6 6.8 1.0
CA h:CYS23 4.7 5.8 1.0
O h:CYS74 4.8 5.8 1.0
N h:ARG28 4.8 5.8 1.0
N h:ALA27 4.8 5.8 1.0
C h:ASN25 4.8 7.1 1.0
C h:CYS74 5.0 5.8 1.0

Zinc binding site 2 out of 3 in 6zxh

Go back to Zinc Binding Sites List in 6zxh
Zinc binding site 2 out of 3 in the Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
d:Zn101

b:27.8
occ:1.00
SG d:CYS42 2.4 5.8 1.0
SG d:CYS39 2.4 5.8 1.0
SG d:CYS24 2.4 5.8 1.0
SG d:CYS21 2.9 5.8 1.0
CB d:CYS42 3.2 5.8 1.0
CB d:CYS24 3.5 5.8 1.0
CB d:CYS39 3.6 5.8 1.0
CB d:CYS21 3.7 5.8 1.0
N d:CYS42 4.1 5.8 1.0
N d:CYS24 4.2 5.8 1.0
CA d:CYS42 4.3 5.8 1.0
O2' 2:G1495 4.3 5.8 1.0
N d:CYS39 4.3 5.8 1.0
CA d:CYS24 4.4 5.8 1.0
CA d:CYS39 4.5 5.8 1.0
N3 2:G1495 4.7 5.8 1.0
CB d:VAL23 4.7 5.8 1.0
O d:CYS39 4.7 5.8 1.0
N2 2:G1495 4.8 5.8 1.0
C d:CYS39 4.9 5.8 1.0
CB d:ASN26 4.9 5.8 1.0

Zinc binding site 3 out of 3 in 6zxh

Go back to Zinc Binding Sites List in 6zxh
Zinc binding site 3 out of 3 in the Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of A Late Human Pre-40S Ribosomal Subunit - State H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
f:Zn500

b:47.2
occ:1.00
SG f:CYS144 2.4 24.8 1.0
SG f:CYS121 2.4 21.9 1.0
SG f:CYS126 2.4 26.8 1.0
SG f:CYS141 2.5 22.0 1.0
CB f:CYS126 2.5 26.8 1.0
CB f:CYS144 3.4 24.8 1.0
CB f:CYS121 3.5 21.9 1.0
CB f:CYS141 3.5 22.0 1.0
CA f:CYS126 3.9 26.8 1.0
N f:CYS144 4.1 24.8 1.0
CB f:SER123 4.2 21.1 1.0
N f:CYS126 4.2 26.8 1.0
CA f:CYS144 4.3 24.8 1.0
O f:CYS126 4.4 26.8 1.0
C f:CYS126 4.6 26.8 1.0
CA f:CYS121 4.9 21.9 1.0
CB f:LEU146 4.9 22.4 1.0
OG f:SER123 4.9 21.1 1.0
C f:LYS143 4.9 23.8 1.0
CB f:LYS143 4.9 23.8 1.0
CA f:CYS141 4.9 22.0 1.0
C f:CYS144 5.0 24.8 1.0

Reference:

M.Ameismeier, I.Zemp, J.Van Den Heuvel, M.Thoms, O.Berninghausen, U.Kutay, R.Beckmann. Structural Basis For the Final Steps of Human 40S Ribosome Maturation. Nature V. 587 683 2020.
ISSN: ESSN 1476-4687
PubMed: 33208940
DOI: 10.1038/S41586-020-2929-X
Page generated: Tue Oct 29 16:09:25 2024

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