Manganese in PDB 1jlm: I-Domain From Integrin CR3, MN2+ Bound

The structure of I-Domain From Integrin CR3, MN2+ Bound, PDB code: 1jlm was solved by J.-O.Lee, R.Liddington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	135.000, 37.100, 38.500, 90.00, 92.60, 90.00
R / Rfree (%)	21.9 / n/a

The binding sites of Manganese atom in the I-Domain From Integrin CR3, MN2+ Bound (pdb code 1jlm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the I-Domain From Integrin CR3, MN2+ Bound, PDB code: 1jlm:

Manganese binding site 1 out of 1 in the I-Domain From Integrin CR3, MN2+ Bound


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of I-Domain From Integrin CR3, MN2+ Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn400 b:25.8 occ:1.00 O A:HOH404 2.1 17.3 1.0 OG A:SER144 2.1 19.4 1.0 O A:HOH409 2.1 16.4 1.0 OD1 A:ASP242 2.3 18.0 1.0 OG A:SER142 2.3 6.5 1.0 O A:HOH408 2.4 36.5 1.0 CG A:ASP242 3.2 16.1 1.0 CB A:SER144 3.4 16.6 1.0 OD2 A:ASP242 3.4 15.4 1.0 CB A:SER142 3.5 6.3 1.0 OG1 A:THR209 4.0 13.6 1.0 OD2 A:ASP140 4.0 9.8 1.0 C A:ASP242 4.3 10.7 1.0 N A:GLY243 4.3 11.3 1.0 OD1 A:ASP140 4.4 7.8 1.0 O A:ASP242 4.4 11.3 1.0 N A:SER144 4.4 14.3 1.0 CA A:GLY243 4.4 11.2 1.0 CA A:SER144 4.5 11.1 1.0 O A:HOH406 4.5 27.9 1.0 CB A:ASP242 4.5 13.2 1.0 CG A:ASP140 4.6 11.7 1.0 CA A:SER142 4.6 12.1 1.0 O A:HOH405 4.7 13.2 1.0 CG1 A:ILE145 4.8 6.2 1.0 C A:SER142 4.8 12.8 1.0 CA A:ASP242 4.8 11.5 1.0 O A:HOH402 4.9 15.9 1.0 N A:ILE145 5.0 12.2 1.0 O A:SER142 5.0 7.6 1.0 C A:SER144 5.0 11.7 1.0 CD1 A:ILE145 5.0 3.4 1.0

J.O.Lee, L.A.Bankston, M.A.Arnaout, R.C.Liddington. Two Conformations of the Integrin A-Domain (I-Domain): A Pathway For Activation? Structure V. 3 1333 1995.
ISSN: ISSN 0969-2126
PubMed: 8747460
DOI: 10.1016/S0969-2126(01)00271-4