Human Serum Albumin Bound to Cerastecin Compound 5e. Determined by X-ray diffraction at 1.91 Å resolution. Released 4 Sept 2024.
Explore 9CSG in 3D Show helices and sheets RCSB PDB PDBe
9CSG contains 36 α-helices and 0 β-strands across 1 chain. 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 | 6-14 | 9 | |
| α-helix | 16-30 | 15 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-74 | 9 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 94 | 1 | |
| α-helix | 97-104 | 8 | |
| α-helix | 112-114 | 3 | |
| α-helix | 120-129 | 10 | |
| α-helix | 131-145 | 15 | |
| α-helix | 151-168 | 18 | |
| α-helix | 174-222 | 49 | |
| α-helix | 228-247 | 20 | |
| α-helix | 250-266 | 17 | |
| α-helix | 268-271 | 4 | |
| α-helix | 276-280 | 5 | |
| α-helix | 283-291 | 9 | |
| α-helix | 293-299 | 7 | |
| α-helix | 306 | 1 | |
| α-helix | 307-311 | 5 | |
| α-helix | 315-321 | 7 | |
| α-helix | 323-337 | 15 | |
| α-helix | 343-360 | 18 | |
| α-helix | 366-370 | 5 | |
| α-helix | 374-414 | 41 | |
| α-helix | 420-438 | 19 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-477 | 7 | |
| α-helix | 484-489 | 6 | |
| α-helix | 491-493 | 3 | |
| α-helix | 497-502 | 6 | |
| α-helix | 512-515 | 4 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-558 | 18 | |
| α-helix | 564-583 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Albumin | A | protein | 582 | Homo sapiens | P02768 (AlphaFold model) |
>9CSG_1 Albumin (chains A) HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENC DKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDV MCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKL DELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADL PSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCA AADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPT LVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKE QLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALG
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1AZR | 2-(4-butylbenzene-1-sulfonamido)-5-(4-{3-carboxy-4-[4-(2-methoxyethyl)benzene-1… | C37 H40 N4 O11 S2 | 1 |
| MYR | Myristic acid | C14 H28 O2 | 6 |
Cerastecin Inhibition of the Lipooligosaccharide Transporter MsbA to Combat Acinetobacter baumannii : From Screening Impurity to In Vivo Efficacy. Skudlarek, J.W., Cooke, A.J., Mitchell, H.J. et al. J Med Chem (2024) 67:15620-15675. DOI 10.1021/acs.jmedchem.4c01277 · PubMed
Other PDB entries of the same protein (UniProt P02768 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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