5TBK: Human importin a3
Crystal structure of human importin a3 bound to RCC1. Determined by X-ray diffraction at 3.45 Å resolution. Released 13 Sept 2017.
- Method
- X-ray diffraction
- Resolution
- 3.45 Å
- Organism
- Homo sapiens
- Chains
- 16
- Atoms
- 50,677
- Mol. weight
- 823.73 kDa
- Released
- 13 Sept 2017
Explore 5TBK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5TBK contains 329 α-helices and 249 β-strands across 16 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.
Chain A: 33 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 76-79 | 4 | |
| α-helix | 85-96 | 12 | |
| α-helix | 98-103 | 6 | |
| α-helix | 107-113 | 7 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-336 | 6 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chain B: 32 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 76-79 | 4 | |
| α-helix | 85-100 | 16 | |
| α-helix | 105-106 | 2 | |
| α-helix | 112-124 | 13 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-464 | 7 | |
| α-helix | 471-484 | 14 | |
Chain C: 31 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 76-79 | 4 | |
| α-helix | 85-100 | 16 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chain D: 33 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 75-79 | 5 | |
| α-helix | 85-96 | 12 | |
| α-helix | 98-103 | 6 | |
| α-helix | 108-113 | 6 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-336 | 6 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chain E: 32 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 75-79 | 5 | |
| α-helix | 85-100 | 16 | |
| α-helix | 104-106 | 3 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chains F and G: 31 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 75-79 | 5 | |
| α-helix | 85-100 | 16 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chain H: 31 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 76-79 | 4 | |
| α-helix | 85-100 | 16 | |
| α-helix | 115-124 | 10 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-154 | 8 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-187 | 17 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-336 | 6 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-365 | 8 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-408 | 8 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 | |
Chain I: 10 helices, 31 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-10 | 5 | |
| α-helix | 12-14 | 3 | |
| β-strand | 35 | 1 | 1 |
| β-strand | 36-42 | 7 | 2 |
| β-strand | 56-62 | 7 | 2 |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| β-strand | 88-92 | 5 | 1 |
| β-strand | 113-114 | 2 | 1 |
| β-strand | 121-126 | 6 | 3 |
| β-strand | 130-135 | 6 | 3 |
| β-strand | 140-144 | 5 | 3 |
| β-strand | 146 | 1 | 4 |
| β-strand | 154 | 1 | 4 |
| β-strand | 162-168 | 7 | 3 |
| β-strand | 174-179 | 6 | 5 |
| β-strand | 183-188 | 6 | 5 |
| β-strand | 193-197 | 5 | 5 |
| α-helix | 209-211 | 3 | |
| α-helix | 220-223 | 4 | |
| β-strand | 227 | 1 | 5 |
| β-strand | 244-247 | 4 | 6 |
| β-strand | 251-255 | 5 | 6 |
| β-strand | 261-265 | 5 | 6 |
| β-strand | 280-285 | 6 | 6 |
| α-helix | 287-289 | 3 | |
| β-strand | 296-301 | 6 | 7 |
| β-strand | 305-310 | 6 | 7 |
| β-strand | 315-319 | 5 | 7 |
| α-helix | 322-324 | 3 | |
| α-helix | 332-334 | 3 | |
| β-strand | 335-340 | 6 | 7 |
| β-strand | 347-352 | 6 | 8 |
| β-strand | 356-361 | 6 | 8 |
| β-strand | 366-370 | 5 | 8 |
| α-helix | 384 | 1 | |
| β-strand | 385-390 | 6 | 8 |
| α-helix | 391 | 1 | |
| α-helix | 394-396 | 3 | |
| β-strand | 399-406 | 8 | 2 |
| β-strand | 410-417 | 8 | 2 |
7 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Importin subunit alpha-3 | A, B, C, D, E, F, G, H | protein | 521 | Homo sapiens | O00629 (AlphaFold model) |
| Regulator of chromosome condensation | I, J, K, L, M, N, O, P | protein | 421 | Homo sapiens | P18754 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>5TBK_1 Importin subunit alpha-3 (chains A, B, C, D, E, F, G, H)
MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDS
DIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILV
HCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWA
LGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETI
QEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKV
QTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQ
VQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLL
TVKDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEI
IDQFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF
Sequence of entity 2 (I, J, K, L, M, N, O, P), FASTA
>5TBK_2 Regulator of chromosome condensation (chains I, J, K, L, M, N, O, P)
MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKP
ALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEK
VVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASG
NDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHV
RFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFS
GGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAV
TKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQ
S
Primary citation
Three-dimensional context rather than NLS amino acid sequence determines importin alpha subtype specificity for RCC1. Sankhala, R.S., Lokareddy, R.K., Begum, S. et al. Nat Commun (2017) 8:979-979. DOI 10.1038/s41467-017-01057-7 · PubMed
Other PDB entries of the same protein (UniProt O00629 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6BW9 1.6 Å, Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 1
- 8HKW 1.9 Å, Crystal structure of importin-alpha3 bound to the 53BP1 nuclear localization signal
- 7LFC 2.1 Å, Structure of importin a3 bound to p50 NLS
- 7RG5 2.15 Å, Importin alpha3 in complex with p50 NLS
- 6BWA 2.2 Å, Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 2
- 6BVV 2.3 Å, Nipah virus W protein C-terminus in complex with Importin alpha 3
- 6BVZ 2.3 Å, Importin alpha 3 in cargo free state
- 6BWB 2.3 Å, Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 3
- 6WX8 2.3 Å, SOX2 bound to Importin-alpha 3
- 7RFY 2.5 Å, Importin alpha3 in complex with MERS ORF4B
- 7JJL 2.6 Å, Crystal structure of Importin Alpha 3 in complex with human LSD1 NLS
- 4UAE 2.7 Å, Importin alpha 3 delta IBB in complex with Influenza PB2 Nuclear Localization Domain
Browse structure collections
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