Structure of Human Serum Albumin in complex with Aristolochic Acid at 1.9 A resolution. Determined by X-ray diffraction at 1.9 Å resolution. Released 26 Jun 2024.
Explore 8RGK in 3D Show helices and sheets RCSB PDB PDBe
8RGK contains 77 α-helices and 0 β-strands across 2 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 | 6-14 | 9 | |
| α-helix | 16-30 | 15 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-75 | 10 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 95-104 | 10 | |
| 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 | 268-270 | 3 | |
| α-helix | 276-279 | 4 | |
| α-helix | 283-291 | 9 | |
| α-helix | 293-299 | 7 | |
| α-helix | 302-304 | 3 | |
| 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 | 366-369 | 4 | |
| α-helix | 373-376 | 4 | |
| α-helix | 377-397 | 21 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-437 | 18 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-478 | 8 | |
| α-helix | 481-483 | 3 | |
| α-helix | 484-489 | 6 | |
| α-helix | 491-493 | 3 | |
| α-helix | 497-502 | 6 | |
| α-helix | 511-513 | 3 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-558 | 18 | |
| α-helix | 565-582 | 18 |
| 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 | 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 | 268-270 | 3 | |
| α-helix | 276-279 | 4 | |
| α-helix | 283-291 | 9 | |
| α-helix | 293-299 | 7 | |
| α-helix | 302-304 | 3 | |
| 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 | 366-369 | 4 | |
| α-helix | 373-376 | 4 | |
| α-helix | 377-397 | 21 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-437 | 18 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-478 | 8 | |
| α-helix | 481-489 | 9 | |
| α-helix | 500-502 | 3 | |
| α-helix | 505-507 | 3 | |
| α-helix | 511-515 | 5 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-558 | 18 | |
| α-helix | 565-581 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serum albumin | A, B | protein | 609 | Homo sapiens | P02768 (AlphaFold model) |
>8RGK_1 Serum albumin (chains A, B) MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV AASQAALGL
| ID | Name | Formula | Copies |
|---|---|---|---|
| GOQ | 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid | C17 H11 N O7 | 1 |
| MYR | Myristic acid | C14 H28 O2 | 13 |
Water and common crystallization additives (EDO) are not listed.
Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin. Pomyalov, S., Minetti, C.A., Remeta, D.P. et al. J Biol Chem (2024) 300:107358-107358. DOI 10.1016/j.jbc.2024.107358 · 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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