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Nickel in PDB 7oxh: Ttslyd with Pseudo-Wild-Type S2 Peptide

Enzymatic activity of Ttslyd with Pseudo-Wild-Type S2 Peptide

All present enzymatic activity of Ttslyd with Pseudo-Wild-Type S2 Peptide:
5.2.1.8;

Protein crystallography data

The structure of Ttslyd with Pseudo-Wild-Type S2 Peptide, PDB code: 7oxh was solved by S.Pazicky, J.Lei, C.Loew, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.63 / 1.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 49.225, 49.225, 131.214, 90, 90, 120
R / Rfree (%) 20.3 / 23.8

Other elements in 7oxh:

The structure of Ttslyd with Pseudo-Wild-Type S2 Peptide also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Ttslyd with Pseudo-Wild-Type S2 Peptide (pdb code 7oxh). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Ttslyd with Pseudo-Wild-Type S2 Peptide, PDB code: 7oxh:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in 7oxh

Go back to Nickel Binding Sites List in 7oxh
Nickel binding site 1 out of 2 in the Ttslyd with Pseudo-Wild-Type S2 Peptide


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Ttslyd with Pseudo-Wild-Type S2 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni205

b:53.8
occ:1.00
OE2 A:GLU97 2.0 31.2 1.0
O A:HOH346 2.2 31.0 1.0
CD A:GLU97 3.1 31.5 1.0
OE1 A:GLU97 3.5 31.9 1.0
ND2 A:ASN99 4.0 31.4 1.0
OD1 A:ASN99 4.1 31.2 1.0
CG A:GLU97 4.4 37.1 1.0
CG A:ASN99 4.5 30.0 1.0

Nickel binding site 2 out of 2 in 7oxh

Go back to Nickel Binding Sites List in 7oxh
Nickel binding site 2 out of 2 in the Ttslyd with Pseudo-Wild-Type S2 Peptide


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Ttslyd with Pseudo-Wild-Type S2 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni206

b:65.5
occ:0.50
O A:HOH307 2.2 68.7 1.0
O A:HOH324 2.3 51.5 0.5
O A:HOH343 2.6 67.6 1.0
OE2 A:GLU131 4.2 41.9 1.0
OE1 A:GLU131 4.2 50.8 1.0
NH1 A:ARG12 4.6 59.9 1.0
CD A:GLU131 4.6 42.8 1.0
O1 A:PEG203 4.7 79.0 1.0

Reference:

S.Pazicky, A.A.Werle, J.Lei, C.Low, U.Weininger. Impact of Distant Peptide Substrate Residues on Enzymatic Activity of Slyd. Cell.Mol.Life Sci. V. 79 138 2022.
ISSN: ESSN 1420-9071
PubMed: 35184231
DOI: 10.1007/S00018-022-04179-4
Page generated: Mon Aug 18 21:57:02 2025

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