Crystal structure of UPLC1 GAP domain. Determined by X-ray diffraction at 2.06 Å resolution. Released 20 Sept 2005.
Explore 2B0O in 3D Show helices and sheets RCSB PDB PDBe
2B0O contains 65 α-helices and 30 β-strands across 4 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 | 424-433 | 10 | |
| β-strand | 440 | 1 | 1 |
| β-strand | 447 | 1 | 1 |
| β-strand | 451-453 | 3 | 2 |
| β-strand | 458-460 | 3 | 2 |
| α-helix | 462-471 | 10 | |
| β-strand | 478-480 | 3 | 2 |
| α-helix | 488-496 | 9 | |
| α-helix | 499-506 | 8 | |
| α-helix | 524-535 | 12 | |
| α-helix | 542-543 | 2 | |
| α-helix | 548-556 | 9 | |
| α-helix | 560-568 | 9 | |
| α-helix | 576 | 1 | |
| β-strand | 577-578 | 2 | 3 |
| β-strand | 586-587 | 2 | 3 |
| α-helix | 589-595 | 7 | |
| α-helix | 602-611 | 10 | |
| α-helix | 625-631 | 7 | |
| α-helix | 635-643 | 9 | |
| α-helix | 658-665 | 8 | |
| α-helix | 668-680 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 425-434 | 10 | |
| β-strand | 440 | 1 | 4 |
| β-strand | 447 | 1 | 4 |
| β-strand | 451-453 | 3 | 5 |
| β-strand | 458-460 | 3 | 5 |
| α-helix | 462-471 | 10 | |
| β-strand | 478-480 | 3 | 5 |
| α-helix | 488-491 | 4 | |
| α-helix | 492-496 | 5 | |
| α-helix | 499-506 | 8 | |
| α-helix | 524-535 | 12 | |
| α-helix | 542-543 | 2 | |
| α-helix | 549-557 | 9 | |
| α-helix | 560-568 | 9 | |
| β-strand | 577 | 1 | 6 |
| β-strand | 587 | 1 | 6 |
| α-helix | 589-595 | 7 | |
| α-helix | 599-601 | 3 | |
| α-helix | 602-611 | 10 | |
| α-helix | 625-631 | 7 | |
| α-helix | 635-643 | 9 | |
| α-helix | 646-648 | 3 | |
| α-helix | 658-665 | 8 | |
| α-helix | 668-678 | 11 | |
| β-strand | 689 | 1 | 7 |
| α-helix | 690-696 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 423-433 | 11 | |
| β-strand | 440 | 1 | 8 |
| β-strand | 447 | 1 | 8 |
| β-strand | 451-453 | 3 | 9 |
| β-strand | 458-460 | 3 | 9 |
| α-helix | 462-471 | 10 | |
| β-strand | 478-480 | 3 | 9 |
| α-helix | 488-496 | 9 | |
| α-helix | 499-506 | 8 | |
| α-helix | 524-532 | 9 | |
| α-helix | 533-537 | 5 | |
| α-helix | 548-556 | 9 | |
| α-helix | 560-568 | 9 | |
| α-helix | 576 | 1 | |
| β-strand | 577 | 1 | 10 |
| α-helix | 578 | 1 | |
| β-strand | 587 | 1 | 10 |
| α-helix | 589-596 | 8 | |
| α-helix | 599-601 | 3 | |
| α-helix | 602-611 | 10 | |
| α-helix | 625-631 | 7 | |
| α-helix | 635-643 | 9 | |
| α-helix | 646-647 | 2 | |
| α-helix | 658-665 | 8 | |
| α-helix | 668-680 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 425-434 | 10 | |
| β-strand | 440 | 1 | 11 |
| β-strand | 447 | 1 | 11 |
| β-strand | 451-453 | 3 | 12 |
| β-strand | 458-460 | 3 | 12 |
| α-helix | 462-471 | 10 | |
| β-strand | 478-480 | 3 | 12 |
| α-helix | 492-496 | 5 | |
| α-helix | 499-506 | 8 | |
| α-helix | 524-535 | 12 | |
| α-helix | 548-556 | 9 | |
| α-helix | 560-568 | 9 | |
| β-strand | 577 | 1 | 13 |
| β-strand | 587 | 1 | 13 |
| α-helix | 589-595 | 7 | |
| α-helix | 599-601 | 3 | |
| α-helix | 602-611 | 10 | |
| α-helix | 625-631 | 7 | |
| α-helix | 635-643 | 9 | |
| α-helix | 658-664 | 7 | |
| α-helix | 668-681 | 14 | |
| β-strand | 687 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| UPLC1 | E, F, G, H | protein | 301 | Homo sapiens | Q8TDY4 (AlphaFold model) |
>2B0O_1 UPLC1 (chains E, F, G, H) MGSSHHHHHHSSGLVPRGSGHDGEPHDLTKLLIAEVKSRPGNSQCCDCGAADPTWLSTNL GVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLPSHGGP KPSAESDMGTRRDYIMAKYVEHRFARRCTPEPQRLWTAICNRDLLSVLEAFANGQDFGQP LPGPDAQAPEELVLHLAVKVANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPD CLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELLEQAQAGTFAFPLHVDYSWVIST E
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Structural analysis of GAP and ankyrin domains of UPLC1. Ismail, S., Shen, L., Arrowsmith, C. et al. To be published.
Other PDB entries of the same protein (UniProt Q8TDY4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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