Crystal Structure of N-terminal Fragments of E1. Determined by X-ray diffraction at 2.75 Å resolution. Released 25 Feb 2015.
Explore 4P22 in 3D Show helices and sheets RCSB PDB PDBe
4P22 contains 36 α-helices and 40 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 | 55-62 | 8 | |
| β-strand | 74-78 | 5 | 1 |
| α-helix | 82-93 | 12 | |
| β-strand | 98-102 | 5 | 1 |
| β-strand | 106 | 1 | 2 |
| α-helix | 107 | 1 | |
| α-helix | 109-112 | 4 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 2 |
| α-helix | 127-136 | 10 | |
| β-strand | 144-147 | 4 | 1 |
| α-helix | 153-156 | 4 | |
| β-strand | 161-164 | 4 | 1 |
| α-helix | 169-181 | 13 | |
| β-strand | 185-192 | 8 | 1 |
| β-strand | 195-201 | 7 | 1 |
| β-strand | 206-210 | 5 | 3 |
| β-strand | 219-224 | 6 | 4 |
| β-strand | 231-234 | 4 | 4 |
| β-strand | 244-251 | 8 | 4 |
| α-helix | 257-259 | 3 | |
| α-helix | 262-264 | 3 | |
| β-strand | 265-269 | 5 | 4 |
| β-strand | 275-276 | 2 | 4 |
| α-helix | 284-286 | 3 | |
| β-strand | 291-296 | 6 | 4 |
| β-strand | 297-301 | 5 | 3 |
| α-helix | 302-305 | 4 | |
| α-helix | 306-311 | 6 | |
| β-strand | 315 | 1 | 1 |
| α-helix | 326-343 | 18 | |
| α-helix | 352-368 | 17 | |
| α-helix | 380-388 | 9 | |
| α-helix | 395-413 | 19 | |
| β-strand | 423-427 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 55-63 | 9 | |
| β-strand | 74-78 | 5 | 5 |
| α-helix | 82-94 | 13 | |
| β-strand | 98-102 | 5 | 5 |
| β-strand | 106 | 1 | 6 |
| α-helix | 107 | 1 | |
| α-helix | 109-111 | 3 | |
| β-strand | 126 | 1 | 6 |
| α-helix | 127-137 | 11 | |
| β-strand | 144-147 | 4 | 5 |
| α-helix | 153-157 | 5 | |
| β-strand | 161-164 | 4 | 5 |
| α-helix | 169-182 | 14 | |
| β-strand | 185-192 | 8 | 5 |
| β-strand | 195-201 | 7 | 5 |
| β-strand | 206-210 | 5 | 7 |
| β-strand | 218-220 | 3 | 8 |
| β-strand | 223-224 | 2 | 9 |
| β-strand | 231-233 | 3 | 9 |
| α-helix | 237-240 | 4 | |
| β-strand | 247-251 | 5 | 8 |
| β-strand | 254 | 1 | 10 |
| α-helix | 258-261 | 4 | |
| α-helix | 263-264 | 2 | |
| β-strand | 265-266 | 2 | 8 |
| β-strand | 268-269 | 2 | 9 |
| β-strand | 274-276 | 3 | 9 |
| α-helix | 284-286 | 3 | |
| β-strand | 288 | 1 | 10 |
| β-strand | 291-296 | 6 | 8 |
| β-strand | 297-301 | 5 | 7 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-311 | 6 | |
| α-helix | 313-314 | 2 | |
| β-strand | 315 | 1 | 5 |
| α-helix | 324-343 | 20 | |
| α-helix | 346-348 | 3 | |
| α-helix | 352-368 | 17 | |
| α-helix | 380-389 | 10 | |
| α-helix | 395-414 | 20 | |
| β-strand | 422-427 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme 1 | A, B | protein | 446 | Homo sapiens | P22314 (AlphaFold model) |
>4P22_1 Ubiquitin-like modifier-activating enzyme 1 (chains A, B) GPHMADLMSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEG LYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLS SQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQL RVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVT CLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVS QVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNDE DAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKAC SGKFMPIMQWLYFDALECLPEDKEVL
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1). Xie, S.T. Biosci Biotechnol Biochem (2014) 78:1542-1549. DOI 10.1080/09168451.2014.923301 · PubMed
Other PDB entries of the same protein (UniProt P22314 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4P22 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.