nuclear Cap Binding Complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Sept 2001.
Explore 1H6K in 3D Show helices and sheets RCSB PDB PDBe
1H6K contains 153 α-helices and 36 β-strands across 6 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 | 28-37 | 10 | |
| α-helix | 46-59 | 14 | |
| α-helix | 61-78 | 18 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 98-117 | 20 | |
| α-helix | 121-136 | 16 | |
| β-strand | 140 | 1 | 1 |
| α-helix | 142-154 | 13 | |
| α-helix | 155-157 | 3 | |
| α-helix | 163-174 | 12 | |
| α-helix | 177-187 | 11 | |
| α-helix | 189-205 | 17 | |
| α-helix | 211-214 | 4 | |
| β-strand | 217 | 1 | 2 |
| β-strand | 226-227 | 2 | 3 |
| α-helix | 228-241 | 14 | |
| α-helix | 252-256 | 5 | |
| α-helix | 262-264 | 3 | |
| β-strand | 266 | 1 | 1 |
| α-helix | 267-270 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-285 | 4 | |
| β-strand | 287-288 | 2 | 3 |
| α-helix | 294-296 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 309-325 | 17 | |
| α-helix | 329-337 | 9 | |
| α-helix | 347-359 | 13 | |
| α-helix | 369-382 | 14 | |
| α-helix | 387-400 | 14 | |
| α-helix | 402-404 | 3 | |
| β-strand | 405 | 1 | 2 |
| α-helix | 407-422 | 16 | |
| α-helix | 430-436 | 7 | |
| α-helix | 444-458 | 15 | |
| α-helix | 462-468 | 7 | |
| α-helix | 471-476 | 6 | |
| α-helix | 478-480 | 3 | |
| α-helix | 498-509 | 12 | |
| α-helix | 514-521 | 8 | |
| α-helix | 541-554 | 14 | |
| α-helix | 559-568 | 10 | |
| α-helix | 570-576 | 7 | |
| α-helix | 580-594 | 15 | |
| α-helix | 598-610 | 13 | |
| α-helix | 616-623 | 8 | |
| α-helix | 626-628 | 3 | |
| α-helix | 635-664 | 30 | |
| α-helix | 692-731 | 40 | |
| α-helix | 738-753 | 16 | |
| α-helix | 755-758 | 4 | |
| α-helix | 759-761 | 3 | |
| α-helix | 762-768 | 7 | |
| α-helix | 776-786 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-37 | 11 | |
| α-helix | 46-58 | 13 | |
| α-helix | 61-78 | 18 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 98-117 | 20 | |
| α-helix | 121-136 | 16 | |
| β-strand | 140 | 1 | 4 |
| α-helix | 142-154 | 13 | |
| α-helix | 155-157 | 3 | |
| α-helix | 163-174 | 12 | |
| α-helix | 177-204 | 28 | |
| α-helix | 211-214 | 4 | |
| β-strand | 217 | 1 | 5 |
| β-strand | 227 | 1 | 6 |
| α-helix | 228-241 | 14 | |
| α-helix | 252-256 | 5 | |
| α-helix | 262-264 | 3 | |
| β-strand | 266 | 1 | 4 |
| α-helix | 267-270 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-285 | 4 | |
| β-strand | 287 | 1 | 6 |
| α-helix | 294-296 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 309-325 | 17 | |
| α-helix | 329-337 | 9 | |
| α-helix | 347-359 | 13 | |
| α-helix | 369-382 | 14 | |
| α-helix | 387-400 | 14 | |
| α-helix | 402-404 | 3 | |
| β-strand | 405 | 1 | 5 |
| α-helix | 407-422 | 16 | |
| α-helix | 430-438 | 9 | |
| α-helix | 444-458 | 15 | |
| α-helix | 462-466 | 5 | |
| α-helix | 471-476 | 6 | |
| α-helix | 478-480 | 3 | |
| α-helix | 498-509 | 12 | |
| α-helix | 514-521 | 8 | |
| α-helix | 541-554 | 14 | |
| α-helix | 559-568 | 10 | |
| α-helix | 570-576 | 7 | |
| α-helix | 580-594 | 15 | |
| α-helix | 598-610 | 13 | |
| α-helix | 616-623 | 8 | |
| α-helix | 626-631 | 6 | |
| α-helix | 635-663 | 29 | |
| α-helix | 690-731 | 42 | |
| α-helix | 738-758 | 21 | |
| α-helix | 759-761 | 3 | |
| α-helix | 762-768 | 7 | |
| α-helix | 776-787 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-37 | 11 | |
| α-helix | 46-58 | 13 | |
| α-helix | 61-78 | 18 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 98-117 | 20 | |
| α-helix | 121-136 | 16 | |
| β-strand | 140 | 1 | 7 |
| α-helix | 142-153 | 12 | |
| α-helix | 154-157 | 4 | |
| α-helix | 163-174 | 12 | |
| α-helix | 177-205 | 29 | |
| α-helix | 211-214 | 4 | |
| β-strand | 217 | 1 | 8 |
| β-strand | 227 | 1 | 9 |
| α-helix | 228-241 | 14 | |
| α-helix | 252-256 | 5 | |
| α-helix | 262-264 | 3 | |
| β-strand | 266 | 1 | 7 |
| α-helix | 267-270 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-285 | 4 | |
| β-strand | 287 | 1 | 9 |
| α-helix | 294-296 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 309-325 | 17 | |
| α-helix | 329-337 | 9 | |
| α-helix | 347-360 | 14 | |
| α-helix | 369-382 | 14 | |
| α-helix | 387-400 | 14 | |
| α-helix | 402-404 | 3 | |
| β-strand | 405 | 1 | 8 |
| α-helix | 407-422 | 16 | |
| α-helix | 430-436 | 7 | |
| α-helix | 444-458 | 15 | |
| α-helix | 462-468 | 7 | |
| α-helix | 471-476 | 6 | |
| α-helix | 478-480 | 3 | |
| α-helix | 498-509 | 12 | |
| α-helix | 514-522 | 9 | |
| α-helix | 541-554 | 14 | |
| α-helix | 559-568 | 10 | |
| α-helix | 570-576 | 7 | |
| α-helix | 580-594 | 15 | |
| α-helix | 598-610 | 13 | |
| α-helix | 616-623 | 8 | |
| α-helix | 626-628 | 3 | |
| α-helix | 635-663 | 29 | |
| α-helix | 692-730 | 39 | |
| α-helix | 738-753 | 16 | |
| α-helix | 755-758 | 4 | |
| α-helix | 759-761 | 3 | |
| α-helix | 762-768 | 7 | |
| α-helix | 776-786 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 41-45 | 5 | 10 |
| α-helix | 53-60 | 8 | |
| α-helix | 61-63 | 3 | |
| β-strand | 66-71 | 6 | 10 |
| β-strand | 84-88 | 5 | 10 |
| α-helix | 91-100 | 10 | |
| β-strand | 105-106 | 2 | 11 |
| β-strand | 109-110 | 2 | 11 |
| β-strand | 112-115 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CBP80 | A, B, C | protein | 757 | HOMO SAPIENS | Q09161 (AlphaFold model) |
| 20 kda nuclear cap binding protein | X, Y, Z | protein | 98 | HOMO SAPIENS | P52298 (AlphaFold model) |
>1H6K_1 CBP80 (chains A, B, C) KTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLL PEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHV IAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFANT ESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSI LCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLH CIIKSHWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIEL CKLQPGSLPQVLAQATEMLYMRLDTMNTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLSQ DPESPKPKFVREVLEKCMRLSYHQRILDIVPPTFSALCPSNPTCIYKYGDESSNSLPGHS VALCLAVAFKSKATNDEIFSILKDVPNPNQDDDDDEGFSFNPLKIEVFVQTLLHLAAKSF SHSFSALAKFHEVFKTLAESDEGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAV ANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHDGVLEEQIE RLQEKVESAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSVLTPWYKNCIERLQQIFLQ HHQIIQQYMVTLENLLFTAELDPHILAVFQQFCALQA
>1H6K_2 20 KDA NUCLEAR CAP BINDING PROTEIN (chains X, Y, Z) DQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKTACG FCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFK
Crystal Structure of the Human Nuclear CAP Binding Complex. Mazza, C., Ohno, M., Segref, A. et al. Mol Cell (2001) 8:383. DOI 10.1016/S1097-2765(01)00299-4 · PubMed
Other PDB entries of the same protein (UniProt Q09161 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1H6K 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.