Iron in PDB 1x71: Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Trencam-3,2-Hopo, A Cepabactin Analogue

The structure of Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Trencam-3,2-Hopo, A Cepabactin Analogue, PDB code: 1x71 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 (°)	114.400, 114.400, 119.000, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 25.7

The binding sites of Iron atom in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Trencam-3,2-Hopo, A Cepabactin Analogue (pdb code 1x71). 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 Trencam-3,2-Hopo, A Cepabactin Analogue, PDB code: 1x71:
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 Trencam-3,2-Hopo, A Cepabactin Analogue


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 Trencam-3,2-Hopo, A Cepabactin Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:72.8 occ:1.00 O4 A:DB1201 2.0 61.1 1.0 O1 A:DB1202 2.0 85.2 1.0 O4 A:DB1202 2.1 84.4 1.0 O1 A:DB1201 2.4 62.7 1.0 C1 A:DB1202 2.9 84.0 1.0 C4 A:DB1202 2.9 83.5 1.0 C4 A:DB1201 3.0 60.3 1.0 C1 A:DB1201 3.1 60.8 1.0 NZ A:LYS134 3.7 37.6 1.0 OH A:TYR106 3.7 30.0 1.0 CE2 A:TYR106 4.2 28.6 1.0 C7 A:DB1202 4.3 83.4 1.0 C16 A:DB1202 4.3 83.7 1.0 C7 A:DB1201 4.3 58.2 1.0 NZ A:LYS125 4.3 34.3 1.0 CZ A:TYR106 4.5 29.6 1.0 C16 A:DB1201 4.5 60.0 1.0 NE A:ARG81 4.7 49.6 1.0 N1 A:DB1202 4.7 81.8 1.0 NH2 A:ARG81 4.9 53.4 1.0 N1 A:DB1201 4.9 63.9 1.0 CE A:LYS134 5.0 34.7 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Trencam-3,2-Hopo, A Cepabactin Analogue


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 Trencam-3,2-Hopo, A Cepabactin Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:0.3 occ:1.00 O4 B:DB1203 2.0 0.6 1.0 O4 B:DB1201 2.0 70.0 1.0 O1 B:DB1203 2.0 99.7 1.0 O1 B:DB1201 2.2 70.8 1.0 C4 B:DB1203 2.7 0.4 1.0 C1 B:DB1203 2.8 0.1 1.0 C4 B:DB1201 2.8 70.1 1.0 C1 B:DB1201 2.9 69.8 1.0 NZ B:LYS134 3.8 54.9 1.0 OH B:TYR106 3.9 43.4 1.0 C7 B:DB1203 4.1 0.1 1.0 C16 B:DB1203 4.1 99.7 1.0 NZ B:LYS125 4.2 43.8 1.0 C7 B:DB1201 4.2 68.9 1.0 C16 B:DB1201 4.3 69.3 1.0 NH1 B:ARG81 4.4 56.1 1.0 N1 B:DB1203 4.5 99.5 1.0 CE2 B:TYR106 4.5 40.4 1.0 N1 B:DB1201 4.6 70.2 1.0 CE B:LYS134 4.7 52.6 1.0 CZ B:TYR106 4.7 41.7 1.0 CE B:LYS125 4.9 41.1 1.0 C19 B:DB1203 4.9 99.5 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Siderocalin (Ngal, Lipocalin 2) Complexed with Trencam-3,2-Hopo, A Cepabactin Analogue


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 Trencam-3,2-Hopo, A Cepabactin Analogue within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe200 b:78.7 occ:1.00 O4 C:DB1201 2.0 62.0 1.0 O1 C:DB1201 2.4 62.6 1.0 C4 C:DB1201 2.9 59.4 1.0 C1 C:DB1201 3.1 60.4 1.0 NH1 C:ARG81 3.5 60.3 1.0 NZ C:LYS134 3.8 33.9 1.0 NZ C:LYS125 4.1 35.4 1.0 OH C:TYR106 4.2 32.9 1.0 C7 C:DB1201 4.2 56.6 1.0 CZ C:ARG81 4.5 59.4 1.0 C16 C:DB1201 4.5 59.3 1.0 CE2 C:TYR106 4.5 29.2 1.0 CE C:LYS125 4.8 30.9 1.0 CE C:LYS134 4.8 28.7 1.0 CZ C:TYR106 4.9 29.6 1.0 CD C:LYS125 4.9 26.4 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