Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Determined by X-ray diffraction at 2.18 Å resolution. Released 31 Jan 1994.
Explore 1LLA in 3D Show helices and sheets RCSB PDB PDBe
1LLA contains 44 α-helices and 23 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 | 3-13 | 11 | |
| α-helix | 16-18 | 3 | |
| α-helix | 33-36 | 4 | |
| α-helix | 41 | 1 | |
| α-helix | 45-47 | 3 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-80 | 11 | |
| α-helix | 86-99 | 14 | |
| α-helix | 101-103 | 3 | |
| α-helix | 106-110 | 5 | |
| α-helix | 111-114 | 4 | |
| α-helix | 116-118 | 3 | |
| α-helix | 122-130 | 9 | |
| α-helix | 141-142 | 2 | |
| β-strand | 143-146 | 4 | 1 |
| α-helix | 156-160 | 5 | |
| α-helix | 161-164 | 4 | |
| α-helix | 167-179 | 13 | |
| α-helix | 186-189 | 4 | |
| α-helix | 196-217 | 22 | |
| α-helix | 221-225 | 5 | |
| α-helix | 232 | 1 | |
| β-strand | 233 | 1 | 2 |
| α-helix | 234-235 | 2 | |
| β-strand | 236 | 1 | 3 |
| β-strand | 241-242 | 2 | 4 |
| β-strand | 247-248 | 2 | 4 |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 3 |
| β-strand | 256 | 1 | 2 |
| α-helix | 266-282 | 17 | |
| β-strand | 284-286 | 3 | 5 |
| β-strand | 292-294 | 3 | 5 |
| α-helix | 300-309 | 10 | |
| α-helix | 317-320 | 4 | |
| α-helix | 323-332 | 10 | |
| α-helix | 343-345 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 354-356 | 3 | |
| α-helix | 358-375 | 18 | |
| α-helix | 379-382 | 4 | |
| α-helix | 383-386 | 4 | |
| β-strand | 391-399 | 9 | 6 |
| β-strand | 405-416 | 12 | 1 |
| β-strand | 429-438 | 10 | 1 |
| β-strand | 442-449 | 8 | 6 |
| β-strand | 455-465 | 11 | 1 |
| β-strand | 467 | 1 | 7 |
| α-helix | 472 | 1 | |
| β-strand | 473 | 1 | 7 |
| α-helix | 474-475 | 2 | |
| α-helix | 476-482 | 7 | |
| α-helix | 483 | 1 | |
| β-strand | 484-493 | 10 | 1 |
| β-strand | 496-503 | 8 | 6 |
| α-helix | 504-506 | 3 | |
| β-strand | 510-511 | 2 | 8 |
| α-helix | 517-521 | 5 | |
| β-strand | 538-539 | 2 | 8 |
| α-helix | 540-542 | 3 | |
| β-strand | 548 | 1 | 1 |
| β-strand | 552-562 | 11 | 1 |
| α-helix | 563-566 | 4 | |
| α-helix | 580-583 | 4 | |
| α-helix | 595 | 1 | |
| α-helix | 609-611 | 3 | |
| β-strand | 617-626 | 10 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hemocyanin (subunit type II) | A | protein | 628 | Limulus polyphemus | P04253 (AlphaFold model) |
>1LLA_1 HEMOCYANIN (SUBUNIT TYPE II) (chains A) TLHDKQIRICHLFEQLSSATVIGDGDKHKHSDRLKNVGKLQPGAIFSCFHPDHLEEARHL YEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIFPDKFI PSAAINEAFKKAHVRPEFDESPILVDVQDTGNILDPEYRLAYYREDVGINAHHWHWHLVY PSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLAGYAPHL THVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGYVISEDGSHKTLDELHG TDILGALVESSYESVNHEYYGNLHNWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIF YNWHRFIDNIFHEYKNTLKPYDHDVLNFPDIQVQDVTLHARVDNVVHTFMREQELELKHG INPGNARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDELGNEIKADELR RTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDLLHGVGLNEHKSEYCSCGWPS HLLVPKGNIKGMEYHLFVMLTDWDKDKVDGSESVACVDAVSYCGARDHKYPDKKPMGFPF DRPIHTEHISDFLTNNMFIKDIKIKFHE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CU | Copper (II) ion | Cu | 2 |
Water and common crystallization additives (CL, NA) are not listed.
Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation. Hazes, B., Magnus, K.A., Bonaventura, C. et al. Protein Sci (1993) 2:597-619. PubMed
Other PDB entries of the same protein (UniProt P04253 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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