Atomistry » Manganese » PDB 8q1x-8sp5 » 8sks
Atomistry »
  Manganese »
    PDB 8q1x-8sp5 »
      8sks »

Manganese in PDB 8sks: Human Liver Mitochondrial Superoxide Dismutase [Mn]

Enzymatic activity of Human Liver Mitochondrial Superoxide Dismutase [Mn]

All present enzymatic activity of Human Liver Mitochondrial Superoxide Dismutase [Mn]:
1.15.1.1;

Manganese Binding Sites:

The binding sites of Manganese atom in the Human Liver Mitochondrial Superoxide Dismutase [Mn] (pdb code 8sks). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Human Liver Mitochondrial Superoxide Dismutase [Mn], PDB code: 8sks:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 8sks

Go back to Manganese Binding Sites List in 8sks
Manganese binding site 1 out of 4 in the Human Liver Mitochondrial Superoxide Dismutase [Mn]


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Liver Mitochondrial Superoxide Dismutase [Mn] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:105.7
occ:1.00
OD2 A:ASP183 1.9 97.7 1.0
NE2 A:HIS50 2.0 93.8 1.0
NE2 A:HIS187 2.0 95.1 1.0
NE2 A:HIS98 2.2 96.5 1.0
CE1 A:HIS50 2.8 93.8 1.0
CE1 A:HIS187 3.0 95.1 1.0
CD2 A:HIS187 3.0 95.1 1.0
CG A:ASP183 3.1 97.7 1.0
CE1 A:HIS98 3.1 96.5 1.0
CD2 A:HIS98 3.1 96.5 1.0
CD2 A:HIS50 3.1 93.8 1.0
OD1 A:ASP183 3.6 97.7 1.0
ND1 A:HIS50 4.0 93.8 1.0
ND1 A:HIS187 4.1 95.1 1.0
ND1 A:HIS98 4.1 96.5 1.0
CG A:HIS187 4.2 95.1 1.0
CG A:HIS50 4.2 93.8 1.0
CG A:HIS98 4.2 96.5 1.0
CB A:ASP183 4.3 97.7 1.0
CZ2 A:TRP147 4.3 99.7 1.0
CB A:TRP185 4.5 98.9 1.0
NE2 A:GLN167 4.6 102.9 1.0
CG A:TRP185 4.8 98.9 1.0
CH2 A:TRP147 5.0 99.7 1.0

Manganese binding site 2 out of 4 in 8sks

Go back to Manganese Binding Sites List in 8sks
Manganese binding site 2 out of 4 in the Human Liver Mitochondrial Superoxide Dismutase [Mn]


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Liver Mitochondrial Superoxide Dismutase [Mn] within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn301

b:105.7
occ:1.00
OD2 B:ASP183 1.9 97.7 1.0
NE2 B:HIS50 2.0 93.8 1.0
NE2 B:HIS187 2.0 95.1 1.0
NE2 B:HIS98 2.2 96.5 1.0
CE1 B:HIS50 2.8 93.8 1.0
CE1 B:HIS187 3.0 95.1 1.0
CD2 B:HIS187 3.0 95.1 1.0
CG B:ASP183 3.1 97.7 1.0
CE1 B:HIS98 3.1 96.5 1.0
CD2 B:HIS98 3.1 96.5 1.0
CD2 B:HIS50 3.1 93.8 1.0
OD1 B:ASP183 3.6 97.7 1.0
ND1 B:HIS50 4.0 93.8 1.0
ND1 B:HIS187 4.1 95.1 1.0
ND1 B:HIS98 4.1 96.5 1.0
CG B:HIS187 4.2 95.1 1.0
CG B:HIS50 4.2 93.8 1.0
CG B:HIS98 4.2 96.5 1.0
CB B:ASP183 4.3 97.7 1.0
CZ2 B:TRP147 4.3 99.7 1.0
CB B:TRP185 4.5 98.9 1.0
NE2 B:GLN167 4.6 102.9 1.0
CG B:TRP185 4.8 98.9 1.0
CH2 B:TRP147 5.0 99.7 1.0

Manganese binding site 3 out of 4 in 8sks

Go back to Manganese Binding Sites List in 8sks
Manganese binding site 3 out of 4 in the Human Liver Mitochondrial Superoxide Dismutase [Mn]


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Human Liver Mitochondrial Superoxide Dismutase [Mn] within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn301

b:105.7
occ:1.00
OD2 C:ASP183 1.9 97.7 1.0
NE2 C:HIS50 2.0 93.8 1.0
NE2 C:HIS187 2.0 95.1 1.0
NE2 C:HIS98 2.2 96.5 1.0
CE1 C:HIS50 2.8 93.8 1.0
CE1 C:HIS187 3.0 95.1 1.0
CD2 C:HIS187 3.0 95.1 1.0
CG C:ASP183 3.1 97.7 1.0
CE1 C:HIS98 3.1 96.5 1.0
CD2 C:HIS98 3.1 96.5 1.0
CD2 C:HIS50 3.1 93.8 1.0
OD1 C:ASP183 3.6 97.7 1.0
ND1 C:HIS50 4.0 93.8 1.0
ND1 C:HIS187 4.1 95.1 1.0
ND1 C:HIS98 4.1 96.5 1.0
CG C:HIS187 4.2 95.1 1.0
CG C:HIS50 4.2 93.8 1.0
CG C:HIS98 4.2 96.5 1.0
CB C:ASP183 4.3 97.7 1.0
CZ2 C:TRP147 4.3 99.7 1.0
CB C:TRP185 4.5 98.9 1.0
NE2 C:GLN167 4.6 102.9 1.0
CG C:TRP185 4.8 98.9 1.0
CH2 C:TRP147 5.0 99.7 1.0

Manganese binding site 4 out of 4 in 8sks

Go back to Manganese Binding Sites List in 8sks
Manganese binding site 4 out of 4 in the Human Liver Mitochondrial Superoxide Dismutase [Mn]


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Human Liver Mitochondrial Superoxide Dismutase [Mn] within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn301

b:105.7
occ:1.00
OD2 D:ASP183 1.9 97.7 1.0
NE2 D:HIS50 2.0 93.8 1.0
NE2 D:HIS187 2.0 95.1 1.0
NE2 D:HIS98 2.2 96.5 1.0
CE1 D:HIS50 2.8 93.8 1.0
CE1 D:HIS187 3.0 95.1 1.0
CD2 D:HIS187 3.0 95.1 1.0
CG D:ASP183 3.1 97.7 1.0
CE1 D:HIS98 3.1 96.5 1.0
CD2 D:HIS98 3.1 96.5 1.0
CD2 D:HIS50 3.1 93.8 1.0
OD1 D:ASP183 3.6 97.7 1.0
ND1 D:HIS50 4.0 93.8 1.0
ND1 D:HIS187 4.1 95.1 1.0
ND1 D:HIS98 4.1 96.5 1.0
CG D:HIS187 4.2 95.1 1.0
CG D:HIS50 4.2 93.8 1.0
CG D:HIS98 4.2 96.5 1.0
CB D:ASP183 4.3 97.7 1.0
CZ2 D:TRP147 4.3 99.7 1.0
CB D:TRP185 4.5 98.9 1.0
NE2 D:GLN167 4.6 102.9 1.0
CG D:TRP185 4.8 98.9 1.0
CH2 D:TRP147 5.0 99.7 1.0

Reference:

Z.Zhang, M.L.Tringides, C.E.Morgan, M.Miyagi, J.A.Mears, C.L.Hoppel, E.W.Yu. High-Resolution Structural Proteomics of Mitochondria Using the 'Build and Retrieve' Methodology. Mol.Cell Proteomics V. 22 00666 2023.
ISSN: ESSN 1535-9484
PubMed: 37839702
DOI: 10.1016/J.MCPRO.2023.100666
Page generated: Sun Oct 6 13:47:06 2024

Last articles

Zn in 2YRC
Zn in 2YQP
Zn in 2YR2
Zn in 2YQL
Zn in 2YPT
Zn in 2YPA
Zn in 2YPU
Zn in 2YNW
Zn in 2YNT
Zn in 2YNV
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy