Zinc in PDB 6tc6: Crystal Structure of Mutm From Neisseria Meningitidis

All present enzymatic activity of Crystal Structure of Mutm From Neisseria Meningitidis:
3.2.2.23; 4.2.99.18;

The structure of Crystal Structure of Mutm From Neisseria Meningitidis, PDB code: 6tc6 was solved by J.Silhan, B.Landova, E.Boura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.43 / 2.90
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.378, 37.960, 110.303, 90.00, 89.97, 90.00
R / Rfree (%)	24.5 / 29.8

The binding sites of Zinc atom in the Crystal Structure of Mutm From Neisseria Meningitidis (pdb code 6tc6). 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 Mutm From Neisseria Meningitidis, PDB code: 6tc6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Mutm From Neisseria Meningitidis


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 Mutm From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:83.3 occ:1.00 SG A:CYS270 2.3 78.2 1.0 SG A:CYS273 2.4 66.2 1.0 CB A:CYS253 2.5 53.8 1.0 SG A:CYS250 2.6 64.7 1.0 CB A:CYS270 3.1 71.7 1.0 CB A:CYS250 3.4 62.6 1.0 N A:CYS253 3.5 59.0 1.0 CA A:CYS253 3.6 54.1 1.0 CB A:CYS273 3.6 67.6 1.0 SG A:CYS253 3.7 74.3 1.0 N A:GLY254 4.1 66.2 1.0 N A:CYS273 4.3 75.1 1.0 N A:GLY255 4.3 68.5 1.0 CE1 A:PHE183 4.3 61.0 1.0 C A:CYS253 4.4 62.2 1.0 NH1 A:ARG252 4.4 66.0 1.0 CA A:CYS273 4.5 66.4 1.0 CA A:CYS270 4.6 79.6 1.0 C A:ARG252 4.7 58.9 1.0 CA A:CYS250 4.9 64.7 1.0 CA A:GLY255 4.9 65.2 1.0 CB A:ARG252 4.9 65.0 1.0 CB A:ASN272 5.0 69.1 1.0 C A:ASN272 5.0 71.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Mutm From Neisseria Meningitidis


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 Mutm From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:87.0 occ:1.00 SG C:CYS273 2.3 75.8 1.0 SG C:CYS253 2.3 80.0 1.0 SG C:CYS270 2.3 61.7 1.0 CB C:CYS253 2.8 57.9 1.0 SG C:CYS250 2.9 62.2 1.0 CB C:CYS273 3.4 71.7 1.0 CB C:CYS270 3.5 61.0 1.0 N C:CYS253 3.5 58.9 1.0 CB C:CYS250 3.6 61.5 1.0 CA C:CYS253 3.7 62.9 1.0 N C:CYS273 3.8 76.7 1.0 CA C:CYS273 4.0 67.5 1.0 N C:GLY254 4.3 70.6 1.0 C C:ASN272 4.3 71.3 1.0 CB C:ASN272 4.3 74.6 1.0 N C:GLY255 4.5 66.7 1.0 C C:CYS253 4.5 68.7 1.0 C C:ARG252 4.7 59.1 1.0 CB C:ARG252 4.7 65.5 1.0 CA C:ASN272 4.8 63.6 1.0 NE C:ARG252 4.8 78.7 1.0 CA C:CYS270 4.9 68.5 1.0 CE1 C:PHE183 4.9 58.4 1.0 O C:ASN272 4.9 73.0 1.0 N C:ASN272 4.9 60.7 1.0

B.Landova, J.Silhan. Conformational Changes of Dna Repair Glycosylase Mutm Triggered By Dna Binding. Febs Lett. 2020.
ISSN: ISSN 0014-5793
PubMed: 32598485
DOI: 10.1002/1873-3468.13876