Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S. Determined by X-ray diffraction at 2.1 Å resolution. Released 25 Jan 2005.
Explore 1X89 in 3D Show helices and sheets RCSB PDB PDBe
1X89 contains 28 α-helices and 33 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 29-38 | 10 | 1 |
| α-helix | 48-49 | 2 | |
| β-strand | 50 | 1 | 2 |
| α-helix | 51 | 1 | |
| β-strand | 53-58 | 6 | 1 |
| β-strand | 64-72 | 9 | 1 |
| β-strand | 75-85 | 11 | 1 |
| β-strand | 91-94 | 4 | 1 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-113 | 11 | 1 |
| β-strand | 118-127 | 10 | 1 |
| β-strand | 130-139 | 10 | 1 |
| α-helix | 146-157 | 12 | |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 1 |
| α-helix | 169 | 1 | |
| β-strand | 170 | 1 | 2 |
| α-helix | 171 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 29-38 | 10 | 3 |
| α-helix | 49 | 1 | |
| β-strand | 50 | 1 | 4 |
| α-helix | 51 | 1 | |
| β-strand | 53-58 | 6 | 3 |
| β-strand | 64-72 | 9 | 3 |
| β-strand | 75-85 | 11 | 3 |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-113 | 11 | 3 |
| β-strand | 118-127 | 10 | 3 |
| β-strand | 130-139 | 10 | 3 |
| α-helix | 146-157 | 12 | |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 3 |
| α-helix | 169 | 1 | |
| β-strand | 170 | 1 | 4 |
| α-helix | 171 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 29-38 | 10 | 5 |
| β-strand | 50 | 1 | 6 |
| β-strand | 53-58 | 6 | 5 |
| β-strand | 64-72 | 9 | 5 |
| β-strand | 75-85 | 11 | 5 |
| β-strand | 91-94 | 4 | 5 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-113 | 11 | 5 |
| β-strand | 118-127 | 10 | 5 |
| β-strand | 130-139 | 10 | 5 |
| α-helix | 146-158 | 13 | |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 5 |
| α-helix | 169 | 1 | |
| β-strand | 170 | 1 | 6 |
| α-helix | 171 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neutrophil gelatinase-associated lipocalin | A, B, C | protein | 178 | Homo sapiens | P80188 (AlphaFold model) |
>1X89_1 Neutrophil gelatinase-associated lipocalin (chains A, B, C) QDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKE DKSYNVTSVLFRKKKCDYWIRTFVPGSQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAM VFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
| ID | Name | Formula | Copies |
|---|---|---|---|
| CM1 | Carboxymycobactin S | C36 H49 Fe N5 O12 | 3 |
Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending against Mycobacterial Infections through Iron Sequestration. Holmes, M.A., Paulsene, W., Jide, X. et al. Structure (2005) 13:29-41. DOI 10.1016/j.str.2004.10.009 · PubMed
Other PDB entries of the same protein (UniProt P80188 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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