Recombinant human serum albumin from transgenic plant. Determined by X-ray diffraction at 2.05 Å resolution. Released 2 Nov 2011.
Explore 3SQJ in 3D Show helices and sheets RCSB PDB PDBe
3SQJ contains 73 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 | 66-74 | 9 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 94 | 1 | |
| α-helix | 97-105 | 9 | |
| α-helix | 116-119 | 4 | |
| 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 | 250-265 | 16 | |
| α-helix | 268-270 | 3 | |
| α-helix | 276-280 | 5 | |
| α-helix | 283-291 | 9 | |
| α-helix | 293-298 | 6 | |
| 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 | 343-361 | 19 | |
| α-helix | 366-370 | 5 | |
| α-helix | 373-397 | 25 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-438 | 19 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-478 | 8 | |
| α-helix | 484-489 | 6 | |
| α-helix | 497-502 | 6 | |
| α-helix | 511-515 | 5 | |
| 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 | 66-75 | 10 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 94 | 1 | |
| α-helix | 97-105 | 9 | |
| 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 | 278-280 | 3 | |
| 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 | 323-336 | 14 | |
| α-helix | 343-360 | 18 | |
| α-helix | 366-370 | 5 | |
| α-helix | 373-414 | 42 | |
| α-helix | 420-438 | 19 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-478 | 8 | |
| α-helix | 481-489 | 9 | |
| α-helix | 499-501 | 3 | |
| α-helix | 505-507 | 3 | |
| α-helix | 512-515 | 4 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-558 | 18 | |
| α-helix | 565-579 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serum albumin | A, B | protein | 582 | Homo sapiens | P02768 (AlphaFold model) |
>3SQJ_1 Serum albumin (chains A, B) HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENC DKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDV MCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKL DELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADL PSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCA AADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPT LVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKE QLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALG
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 15 |
Large-scale production of functional human serum albumin from transgenic rice seeds. He, Y., Ning, T., Xie, T. et al. Proc Natl Acad Sci U S A (2011) 108:19078-19083. DOI 10.1073/pnas.1109736108 · 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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