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Zinc in PDB 4ral: Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta

Enzymatic activity of Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta

All present enzymatic activity of Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta:
3.4.24.56;

Protein crystallography data

The structure of Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta, PDB code: 4ral was solved by W.G.Liang, M.Ren, Q.Guo, W.J.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.26 / 3.15
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 263.117, 263.117, 90.850, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 25.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta (pdb code 4ral). 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 Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta, PDB code: 4ral:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4ral

Go back to Zinc Binding Sites List in 4ral
Zinc binding site 1 out of 2 in the Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta


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 Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1101

b:71.6
occ:1.00
O D:LYS45 2.1 72.3 1.0
NE2 A:HIS112 2.1 55.6 1.0
OE1 A:GLU189 2.2 50.9 1.0
NE2 A:HIS108 2.3 36.8 1.0
CE1 A:HIS112 2.9 43.3 1.0
CD A:GLU189 2.9 58.9 1.0
OE2 A:GLU189 3.0 56.5 1.0
C D:LYS45 3.1 79.3 1.0
CD2 A:HIS112 3.2 56.2 1.0
CD2 A:HIS108 3.3 40.8 1.0
CE1 A:HIS108 3.3 46.4 1.0
N D:ARG46 3.9 90.3 1.0
CA D:ARG46 3.9 92.8 1.0
ND1 A:HIS112 4.1 44.2 1.0
N D:LYS45 4.1 85.0 1.0
CA D:LYS45 4.2 78.9 1.0
CG A:HIS112 4.3 49.6 1.0
CG A:GLU189 4.4 52.8 1.0
ND1 A:HIS108 4.4 50.0 1.0
CG A:HIS108 4.4 46.5 1.0
C D:THR44 4.4 84.7 1.0
CE1 A:TYR831 4.5 29.9 1.0
NE2 A:GLN111 4.5 49.6 1.0
CB D:THR44 4.6 74.2 1.0
C D:ARG46 4.7 0.5 1.0
O D:ARG46 4.7 0.9 1.0
O D:THR44 4.7 83.8 1.0
OH A:TYR831 4.7 39.9 1.0
OE1 A:GLN111 4.9 64.1 1.0
CB A:GLU189 4.9 40.1 1.0
CD A:GLN111 4.9 40.7 1.0

Zinc binding site 2 out of 2 in 4ral

Go back to Zinc Binding Sites List in 4ral
Zinc binding site 2 out of 2 in the Crystal Structure of Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta


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 Insulin Degrading Enzyme in Complex with Macrophage Inflammatory Protein 1 Beta within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1101

b:89.1
occ:1.00
NE2 B:HIS112 2.1 42.4 1.0
O E:LYS45 2.2 77.2 1.0
OE1 B:GLU189 2.3 72.2 1.0
NE2 B:HIS108 2.3 50.9 1.0
CE1 B:HIS112 3.0 39.4 1.0
CD B:GLU189 3.0 69.6 1.0
OE2 B:GLU189 3.1 73.0 1.0
CD2 B:HIS112 3.2 54.7 1.0
CD2 B:HIS108 3.2 46.5 1.0
C E:LYS45 3.2 81.7 1.0
CE1 B:HIS108 3.3 60.0 1.0
CA E:ARG46 3.9 80.7 1.0
N E:ARG46 3.9 80.7 1.0
ND1 B:HIS112 4.1 34.8 1.0
CG B:HIS112 4.2 56.9 1.0
N E:LYS45 4.2 94.7 1.0
CA E:LYS45 4.3 83.9 1.0
NE2 B:GLN111 4.3 78.1 1.0
ND1 B:HIS108 4.4 61.1 1.0
CG B:HIS108 4.4 45.1 1.0
CG B:GLU189 4.5 54.8 1.0
CE1 B:TYR831 4.6 33.8 1.0
C E:THR44 4.6 0.8 1.0
O E:ARG46 4.7 74.9 1.0
C E:ARG46 4.7 89.5 1.0
CD B:GLN111 4.7 55.3 1.0
OE1 B:GLN111 4.7 56.8 1.0
CB E:THR44 4.9 90.5 1.0
O E:THR44 4.9 0.2 1.0
CB B:GLU189 5.0 34.1 1.0

Reference:

W.G.Liang, M.Ren, F.Zhao, W.J.Tang. Structures of Human CCL18, CCL3, and CCL4 Reveal Molecular Determinants For Quaternary Structures and Sensitivity to Insulin-Degrading Enzyme. J.Mol.Biol. V. 427 1345 2015.
ISSN: ISSN 0022-2836
PubMed: 25636406
DOI: 10.1016/J.JMB.2015.01.012
Page generated: Sun Oct 27 06:57:37 2024

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