Iron in PDB 1x89: Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S

The structure of Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S, PDB code: 1x89 was solved by M.A.Holmes, W.Paulsene, X.Jide, C.Ratledge, R.K.Strong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	114.200, 114.200, 119.300, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25.1

The binding sites of Iron atom in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S (pdb code 1x89). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S, PDB code: 1x89:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:45.8 occ:1.00 FE A:CM1200 0.0 45.8 1.0 O2 A:CM1200 2.0 44.3 1.0 O36 A:CM1200 2.0 48.9 1.0 O44 A:CM1200 2.1 49.2 1.0 O46 A:CM1200 2.1 49.5 1.0 N11 A:CM1200 2.2 45.9 1.0 O38 A:CM1200 2.2 48.2 1.0 N35 A:CM1200 2.8 49.2 1.0 C45 A:CM1200 2.8 51.5 1.0 C37 A:CM1200 2.9 49.4 1.0 N43 A:CM1200 2.9 52.1 1.0 C3 A:CM1200 3.0 37.8 1.0 C10 A:CM1200 3.0 41.5 1.0 C12 A:CM1200 3.3 47.0 1.0 C8 A:CM1200 3.5 38.1 1.0 N17 A:CM1200 3.6 51.9 1.0 C15 A:CM1200 3.9 49.3 1.0 NZ A:LYS134 3.9 27.6 1.0 C34 A:CM1200 4.2 48.4 1.0 C4 A:CM1200 4.2 35.4 1.0 C42 A:CM1200 4.3 52.7 1.0 O14 A:CM1200 4.3 43.5 1.0 NZ A:LYS125 4.3 33.8 1.0 C47 A:CM1200 4.4 53.2 1.0 C30 A:CM1200 4.4 50.2 1.0 C13 A:CM1200 4.5 46.0 1.0 C40 A:CM1200 4.7 52.8 1.0 C33 A:CM1200 4.8 49.4 1.0 C18 A:CM1200 4.8 53.1 1.0 N29 A:CM1200 4.8 51.0 1.0 C39 A:CM1200 4.9 53.1 1.0 C7 A:CM1200 4.9 32.7 1.0 C31 A:CM1200 5.0 49.5 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:56.6 occ:1.00 FE B:CM1200 0.0 56.6 1.0 O2 B:CM1200 2.0 56.1 1.0 O36 B:CM1200 2.0 57.4 1.0 O44 B:CM1200 2.0 58.2 1.0 O46 B:CM1200 2.1 58.0 1.0 O38 B:CM1200 2.1 58.0 1.0 N11 B:CM1200 2.2 58.0 1.0 N35 B:CM1200 2.7 58.2 1.0 C37 B:CM1200 2.8 58.5 1.0 C45 B:CM1200 2.8 59.6 1.0 N43 B:CM1200 2.9 60.0 1.0 C10 B:CM1200 3.0 57.4 1.0 C3 B:CM1200 3.1 55.2 1.0 C12 B:CM1200 3.3 59.5 1.0 C8 B:CM1200 3.6 55.6 1.0 N17 B:CM1200 3.6 61.4 1.0 C15 B:CM1200 3.8 60.6 1.0 NZ B:LYS134 4.0 42.4 1.0 C34 B:CM1200 4.2 59.9 1.0 C42 B:CM1200 4.3 60.9 1.0 C4 B:CM1200 4.3 55.4 1.0 O14 B:CM1200 4.3 60.5 1.0 C30 B:CM1200 4.3 60.7 1.0 C47 B:CM1200 4.4 60.5 1.0 NZ B:LYS125 4.4 42.3 1.0 O B:HOH204 4.5 59.2 1.0 C13 B:CM1200 4.5 59.4 1.0 C40 B:CM1200 4.7 62.1 1.0 N29 B:CM1200 4.8 62.4 1.0 C18 B:CM1200 4.9 62.2 1.0 C33 B:CM1200 4.9 59.3 1.0 C50 B:CM1200 5.0 60.1 1.0 C31 B:CM1200 5.0 60.6 1.0 CE B:LYS134 5.0 42.9 1.0 C7 B:CM1200 5.0 54.0 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Carboxymycobactin S within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe200 b:39.3 occ:1.00 FE C:CM1200 0.0 39.3 1.0 O2 C:CM1200 2.0 35.0 1.0 O36 C:CM1200 2.0 39.5 1.0 O44 C:CM1200 2.0 39.9 1.0 O46 C:CM1200 2.0 41.4 1.0 O38 C:CM1200 2.1 39.7 1.0 N11 C:CM1200 2.1 36.8 1.0 N35 C:CM1200 2.8 39.1 1.0 C45 C:CM1200 2.8 44.7 1.0 C37 C:CM1200 2.8 40.7 1.0 N43 C:CM1200 2.9 43.8 1.0 C10 C:CM1200 3.0 33.9 1.0 C3 C:CM1200 3.0 27.0 1.0 C12 C:CM1200 3.3 39.6 1.0 C8 C:CM1200 3.5 27.1 1.0 N17 C:CM1200 3.6 45.3 1.0 C15 C:CM1200 3.8 42.8 1.0 NZ C:LYS125 4.0 33.4 1.0 NZ C:LYS134 4.1 22.9 1.0 C34 C:CM1200 4.2 38.2 1.0 C4 C:CM1200 4.3 24.9 1.0 C42 C:CM1200 4.3 45.0 1.0 O14 C:CM1200 4.3 35.8 1.0 C47 C:CM1200 4.4 45.5 1.0 C30 C:CM1200 4.4 41.7 1.0 C13 C:CM1200 4.5 37.5 1.0 C40 C:CM1200 4.7 46.4 1.0 C33 C:CM1200 4.8 38.2 1.0 O C:HOH239 4.9 35.9 1.0 N29 C:CM1200 4.9 42.1 1.0 CE C:LYS134 4.9 21.4 1.0 C31 C:CM1200 4.9 39.2 1.0 C18 C:CM1200 4.9 48.0 1.0 C7 C:CM1200 4.9 24.5 1.0 C48 C:CM1200 5.0 47.6 1.0 O16 C:CM1200 5.0 46.7 1.0

M.A.Holmes, W.Paulsene, X.Jide, C.Ratledge, R.K.Strong. Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending Against Mycobacterial Infections Through Iron Sequestration Structure V. 13 29 2005.
ISSN: ISSN 0969-2126
PubMed: 15642259
DOI: 10.1016/J.STR.2004.10.009