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Magnesium in PDB 6fpy: Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type

Protein crystallography data

The structure of Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type, PDB code: 6fpy was solved by D.C.Briggs, A.J.Day, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.38 / 2.34
Space group P 42
Cell size a, b, c (Å), α, β, γ (°) 158.767, 158.767, 65.371, 90.00, 90.00, 90.00
R / Rfree (%) 23.1 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type (pdb code 6fpy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type, PDB code: 6fpy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6fpy

Go back to Magnesium Binding Sites List in 6fpy
Magnesium binding site 1 out of 2 in the Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:43.5
occ:1.00
OG A:SER302 2.1 62.6 1.0
OG A:SER300 2.2 59.7 1.0
O A:HOH1185 2.2 38.5 1.0
OD1 A:ASP403 2.4 58.4 1.0
HA3 A:GLY404 3.1 69.4 1.0
HG1 A:THR368 3.1 70.0 1.0
CG A:ASP403 3.2 55.2 1.0
CB A:SER300 3.3 50.9 1.0
CB A:SER302 3.4 56.9 1.0
HB2 A:SER300 3.4 61.1 1.0
OD2 A:ASP298 3.5 51.0 1.0
OD2 A:ASP403 3.5 56.7 1.0
HB3 A:SER300 3.5 61.1 1.0
HB3 A:SER302 3.6 68.3 1.0
N A:GLY404 3.7 52.0 1.0
OG1 A:THR368 3.8 58.4 1.0
CA A:GLY404 3.8 57.9 1.0
H A:SER302 3.9 62.6 1.0
HB2 A:SER302 3.9 68.3 1.0
H A:GLY404 3.9 62.4 1.0
HG2 A:MET303 4.0 52.8 1.0
C A:ASP403 4.1 49.7 1.0
H A:ASP403 4.2 53.1 1.0
CG A:ASP298 4.3 53.0 1.0
OD1 A:ASP298 4.4 56.1 1.0
O A:ASP403 4.4 51.4 1.0
CA A:SER302 4.5 50.2 1.0
N A:SER302 4.5 52.2 1.0
HG21 A:THR368 4.5 68.4 1.0
HA2 A:GLY404 4.5 69.4 1.0
H A:MET303 4.5 60.1 1.0
CB A:ASP403 4.5 51.3 1.0
H A:SER300 4.6 65.0 1.0
CA A:SER300 4.6 51.1 1.0
CA A:ASP403 4.7 47.3 1.0
C A:GLY404 4.7 58.5 1.0
N A:ASP403 4.8 44.2 1.0
N A:MET303 4.8 50.1 1.0
HG1 A:THR402 4.9 44.9 1.0
C A:SER300 4.9 51.4 1.0
C A:SER302 4.9 50.1 1.0
CG A:MET303 4.9 44.0 1.0
HB2 A:ASP403 5.0 61.5 1.0
CB A:THR368 5.0 56.9 1.0

Magnesium binding site 2 out of 2 in 6fpy

Go back to Magnesium Binding Sites List in 6fpy
Magnesium binding site 2 out of 2 in the Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Inter-Alpha-Inhibitor Heavy Chain 1, Wild Type within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1001

b:50.8
occ:1.00
OG B:SER302 1.9 74.6 1.0
OG B:SER300 2.3 52.7 1.0
O B:HOH1234 2.3 39.7 1.0
O B:HOH1110 2.4 43.8 1.0
OD1 B:ASP403 2.5 52.9 1.0
CB B:SER302 3.1 64.6 1.0
HB2 B:SER300 3.2 65.7 1.0
HA3 B:GLY404 3.2 67.5 1.0
CG B:ASP403 3.2 50.5 1.0
CB B:SER300 3.3 54.7 1.0
HG1 B:THR368 3.3 74.0 1.0
HB3 B:SER302 3.3 77.5 1.0
OD2 B:ASP403 3.4 54.9 1.0
HB2 B:SER302 3.6 77.5 1.0
HB3 B:SER300 3.6 65.7 1.0
H B:SER302 3.7 69.1 1.0
OD2 B:ASP298 3.7 59.3 1.0
OG1 B:THR368 3.9 61.6 1.0
N B:GLY404 3.9 52.2 1.0
CA B:GLY404 4.0 56.2 1.0
H B:GLY404 4.1 62.6 1.0
HG2 B:MET303 4.1 53.3 1.0
C B:ASP403 4.2 51.6 1.0
CA B:SER302 4.2 61.5 1.0
N B:SER302 4.3 57.6 1.0
H B:ASP403 4.4 51.0 1.0
O B:ASP403 4.5 53.7 1.0
H B:MET303 4.5 66.5 1.0
CB B:ASP403 4.5 48.0 1.0
CG B:ASP298 4.6 57.9 1.0
CA B:SER300 4.6 55.4 1.0
HA2 B:GLY404 4.6 67.5 1.0
OD1 B:ASP298 4.6 61.8 1.0
H B:SER300 4.7 61.7 1.0
C B:SER302 4.8 56.4 1.0
HG21 B:THR368 4.8 61.2 1.0
CA B:ASP403 4.8 44.4 1.0
N B:MET303 4.8 55.4 1.0
C B:SER300 4.8 56.8 1.0
C B:GLY404 4.9 60.4 1.0
HB2 B:ASP403 4.9 57.5 1.0
N B:ASP403 5.0 42.5 1.0

Reference:

D.C.Briggs, A.W.W.Langford-Smith, T.A.Jowitt, C.M.Kielty, J.J.Enghild, C.Baldock, C.M.Milner, A.J.Day. Heavy Chain-1 of Inter-Alpha-Inhibitor Has An Integrin-Like Structure with Immune Regulatory Activities Biorxiv 2019.
DOI: 10.1101/695700
Page generated: Tue Oct 1 00:37:16 2024

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