Crystal structure of KAP beta2-PY-NLS. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 Jul 2012.
Explore 4FDD in 3D Show helices and sheets RCSB PDB PDBe
4FDD contains 67 α-helices and 0 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 | 9-22 | 14 | |
| α-helix | 27-40 | 14 | |
| α-helix | 44-55 | 12 | |
| α-helix | 62-75 | 14 | |
| α-helix | 80-82 | 3 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-117 | 14 | |
| α-helix | 118-122 | 5 | |
| α-helix | 129-137 | 9 | |
| α-helix | 142-159 | 18 | |
| α-helix | 162-165 | 4 | |
| α-helix | 172-179 | 8 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-224 | 12 | |
| α-helix | 229-245 | 17 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-283 | 14 | |
| α-helix | 289-293 | 5 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-319 | 8 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-532 | 14 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-575 | 17 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-601 | 4 | |
| α-helix | 602-628 | 27 | |
| α-helix | 634-636 | 3 | |
| α-helix | 639-655 | 17 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-675 | 8 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-701 | 3 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 748-758 | 11 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-802 | 13 | |
| α-helix | 808-823 | 16 | |
| α-helix | 825-827 | 3 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-872 | 26 | |
| α-helix | 873-875 | 3 | |
| α-helix | 878-886 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 514-521 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 852 | Homo sapiens | Q92973 (AlphaFold model) |
| RNA-binding protein FUS | B | protein | 29 | Homo sapiens | P35637 (AlphaFold model) |
>4FDD_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEGGSGGDDTISDWNLRKCSAAALDVLANVYRDELLPHI LPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSIT CWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPY LAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKD EDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDK DFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKAC FQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEII NRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGIC TMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPL PLKERLAAFYGV
>4FDD_2 RNA-binding protein FUS (chains B) RGGGDRGGFGPGKMDSRGEHRQDRRERPY
Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). Zhang, Z.C., Chook, Y.M. Proc Natl Acad Sci U S A (2012) 109:12017-12021. DOI 10.1073/pnas.1207247109 · PubMed
Other PDB entries of the same protein (UniProt Q92973 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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