Hydroxo bridge met form hemocyanin from limulus. Determined by X-ray diffraction at 2.55 Å resolution. Released 20 Aug 1997.
Explore 1LL1 in 3D Show helices and sheets RCSB PDB PDBe
1LL1 contains 41 α-helices and 27 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 | 3-12 | 10 | |
| α-helix | 22-34 | 13 | |
| α-helix | 45-47 | 3 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-80 | 11 | |
| α-helix | 86-99 | 14 | |
| α-helix | 111-114 | 4 | |
| α-helix | 116-118 | 3 | |
| α-helix | 122-127 | 6 | |
| 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 | 220-225 | 6 | |
| α-helix | 232 | 1 | |
| β-strand | 233 | 1 | 2 |
| α-helix | 234 | 1 | |
| 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 | 300-305 | 6 | |
| α-helix | 306-310 | 5 | |
| 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 | 359-375 | 17 | |
| α-helix | 379-382 | 4 | |
| α-helix | 383-386 | 4 | |
| β-strand | 391-399 | 9 | 6 |
| β-strand | 405-413 | 9 | 7 |
| β-strand | 416 | 1 | 1 |
| β-strand | 429-432 | 4 | 1 |
| β-strand | 433-438 | 6 | 7 |
| β-strand | 442-449 | 8 | 6 |
| β-strand | 455-465 | 11 | 7 |
| β-strand | 467 | 1 | 8 |
| α-helix | 472 | 1 | |
| β-strand | 473 | 1 | 8 |
| α-helix | 474-475 | 2 | |
| α-helix | 476-479 | 4 | |
| α-helix | 483 | 1 | |
| β-strand | 484-493 | 10 | 7 |
| α-helix | 494 | 1 | |
| β-strand | 496-503 | 8 | 6 |
| α-helix | 504-506 | 3 | |
| β-strand | 510-511 | 2 | 9 |
| α-helix | 517-520 | 4 | |
| β-strand | 538-539 | 2 | 9 |
| α-helix | 540-542 | 3 | |
| β-strand | 548 | 1 | 7 |
| β-strand | 552-562 | 11 | 7 |
| α-helix | 563-566 | 4 | |
| β-strand | 575 | 1 | 10 |
| α-helix | 580-583 | 4 | |
| β-strand | 586 | 1 | 10 |
| α-helix | 595 | 1 | |
| α-helix | 609-611 | 3 | |
| β-strand | 617-627 | 11 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metcyanin II | A | protein | 628 | Limulus polyphemus | P04253 (AlphaFold model) |
>1LL1_1 METCYANIN II (chains A) TLHDKQIRVCHLFEQLSSATVIGDGDKHKHSDRLKNVGKLQPGAIFSCFHPDHLEEARHL 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) are not listed.
Crystallographic Studies of Hydroxo, Nitrosyl, Azido and Fluro met Form Hemocyanin Subunit II from Limulus. Liu, S., Ton-that, H., Magnus, K. To be published.
Other PDB entries of the same protein (UniProt P04253 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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