The crystal structure of the zymogen catalytic domain of complement protease C1R. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Jul 2002.
Explore 1GPZ in 3D Show helices and sheets RCSB PDB PDBe
1GPZ contains 29 α-helices and 70 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 |
|---|---|---|---|
| β-strand | 292 | 1 | 1 |
| β-strand | 302-305 | 4 | 2 |
| β-strand | 311 | 1 | 1 |
| β-strand | 316-321 | 6 | 2 |
| β-strand | 325-328 | 4 | 3 |
| β-strand | 333-334 | 2 | 3 |
| β-strand | 337-340 | 4 | 2 |
| β-strand | 341 | 1 | 4 |
| β-strand | 347 | 1 | 4 |
| β-strand | 353-356 | 4 | 3 |
| β-strand | 358 | 1 | 5 |
| α-helix | 362-364 | 3 | |
| β-strand | 368-372 | 5 | 6 |
| β-strand | 380 | 1 | 5 |
| β-strand | 384-389 | 6 | 6 |
| β-strand | 394-397 | 4 | 7 |
| β-strand | 409-412 | 4 | 6 |
| β-strand | 418-420 | 3 | 6 |
| β-strand | 429-432 | 4 | 7 |
| α-helix | 433-434 | 2 | |
| α-helix | 440-442 | 3 | |
| β-strand | 451-452 | 2 | 8 |
| α-helix | 453-454 | 2 | |
| β-strand | 461-465 | 5 | 9 |
| β-strand | 469-475 | 7 | 9 |
| β-strand | 479-482 | 4 | 9 |
| α-helix | 484-486 | 3 | |
| β-strand | 501-504 | 4 | 9 |
| β-strand | 508 | 1 | 10 |
| α-helix | 509-514 | 6 | |
| β-strand | 520-525 | 6 | 9 |
| β-strand | 542-546 | 5 | 9 |
| α-helix | 549-552 | 4 | |
| β-strand | 553 | 1 | 11 |
| β-strand | 556 | 1 | 11 |
| β-strand | 560 | 1 | 8 |
| α-helix | 561-562 | 2 | |
| α-helix | 565-568 | 4 | |
| β-strand | 573-578 | 6 | 8 |
| β-strand | 589 | 1 | 10 |
| β-strand | 591-598 | 8 | 8 |
| α-helix | 599 | 1 | |
| α-helix | 600-604 | 5 | |
| β-strand | 620-624 | 5 | 8 |
| α-helix | 626-633 | 8 | |
| β-strand | 640-645 | 6 | 8 |
| β-strand | 650-657 | 8 | 8 |
| β-strand | 667-672 | 6 | 8 |
| α-helix | 673-676 | 4 | |
| α-helix | 677-683 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 291-292 | 2 | 12 |
| β-strand | 302-304 | 3 | 13 |
| β-strand | 311-312 | 2 | 12 |
| β-strand | 316-321 | 6 | 13 |
| β-strand | 325-329 | 5 | 14 |
| β-strand | 332-334 | 3 | 14 |
| β-strand | 337-340 | 4 | 13 |
| β-strand | 341 | 1 | 15 |
| β-strand | 347 | 1 | 15 |
| β-strand | 353-356 | 4 | 14 |
| α-helix | 357 | 1 | |
| β-strand | 358 | 1 | 16 |
| α-helix | 362-364 | 3 | |
| β-strand | 368-372 | 5 | 17 |
| β-strand | 380 | 1 | 16 |
| β-strand | 384-389 | 6 | 17 |
| β-strand | 394-396 | 3 | 18 |
| β-strand | 409-412 | 4 | 17 |
| β-strand | 418-419 | 2 | 17 |
| β-strand | 430-432 | 3 | 18 |
| α-helix | 433 | 1 | |
| α-helix | 440-443 | 4 | |
| β-strand | 448-452 | 5 | 19 |
| α-helix | 453-454 | 2 | |
| β-strand | 461-465 | 5 | 20 |
| β-strand | 469-475 | 7 | 20 |
| β-strand | 479-482 | 4 | 20 |
| α-helix | 484-486 | 3 | |
| β-strand | 501-504 | 4 | 20 |
| α-helix | 509-514 | 6 | |
| β-strand | 520-525 | 6 | 20 |
| β-strand | 542-546 | 5 | 20 |
| α-helix | 549-552 | 4 | |
| β-strand | 553 | 1 | 21 |
| β-strand | 556 | 1 | 21 |
| β-strand | 560 | 1 | 19 |
| α-helix | 561-562 | 2 | |
| β-strand | 573-578 | 6 | 19 |
| β-strand | 591-598 | 8 | 19 |
| α-helix | 599 | 1 | |
| α-helix | 600-602 | 3 | |
| β-strand | 620-624 | 5 | 19 |
| α-helix | 626-628 | 3 | |
| α-helix | 631-634 | 4 | |
| β-strand | 640-644 | 5 | 19 |
| β-strand | 651-657 | 7 | 19 |
| β-strand | 667-672 | 6 | 19 |
| α-helix | 673-676 | 4 | |
| α-helix | 677-683 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C1R component | A, B | protein | 399 | HOMO SAPIENS | P00736 (AlphaFold model) |
>1GPZ_1 COMPLEMENT C1R COMPONENT (chains A, B) IKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHR AMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGV YTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQQIIGGQKAKMGNFPWQVFTNIHGR GGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDY RQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHD LRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTD RWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
The Crystal Structure of the Zymogen Catalytic Domain of Complement Protease C1R Reveals that a Disruptive Mechanical Stress is Required to Trigger Activation of the C1 Complex. Budayova-Spano, M., Lacroix, M., Thielens, N. et al. EMBO J (2002) 21:231. DOI 10.1093/EMBOJ/21.3.231 · PubMed
Other PDB entries of the same protein (UniProt P00736 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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