2JKT: Ap-2 complex subunit alpha-2
AP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS) EIKRLLSE Q to E mutant. Determined by X-ray diffraction at 3.4 Å resolution. Released 28 Oct 2008.
- Method
- X-ray diffraction
- Resolution
- 3.4 Å
- Organisms
- MUS MUSCULUS, HOMO SAPIENS, RATTUS NORVEGICUS
- Chains
- 10
- Atoms
- 28,120
- Mol. weight
- 412.88 kDa
- Released
- 28 Oct 2008
Explore 2JKT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2JKT contains 191 α-helices and 78 β-strands across 10 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: 37 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-18 | 8 | |
| α-helix | 28-40 | 13 | |
| α-helix | 52-66 | 15 | |
| α-helix | 76-82 | 7 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 188-193 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 201-215 | 15 | |
| α-helix | 225-236 | 12 | |
| β-strand | 248-249 | 2 | 1 |
| β-strand | 252-253 | 2 | 1 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-292 | 19 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-339 | 16 | |
| α-helix | 344-356 | 13 | |
| α-helix | 365-369 | 5 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-394 | 12 | |
| α-helix | 402-414 | 13 | |
| α-helix | 418-435 | 18 | |
| α-helix | 439-449 | 11 | |
| α-helix | 454-456 | 3 | |
| α-helix | 459-471 | 13 | |
| α-helix | 476-486 | 11 | |
| α-helix | 494-506 | 13 | |
| α-helix | 515-517 | 3 | |
| α-helix | 519-530 | 12 | |
| α-helix | 535-551 | 17 | |
| α-helix | 556-560 | 5 | |
| α-helix | 566-569 | 4 | |
| α-helix | 574-588 | 15 | |
| α-helix | 592-598 | 7 | |
| α-helix | 604-606 | 3 | |
| β-strand | 611-614 | 4 | 2 |
Chains B and E: 42 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-23 | 9 | |
| α-helix | 27-39 | 13 | |
| α-helix | 51-55 | 5 | |
| α-helix | 63-74 | 12 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-94 | 7 | |
| α-helix | 100-110 | 11 | |
| α-helix | 116-119 | 4 | |
| α-helix | 123-129 | 7 | |
| α-helix | 135-149 | 15 | |
| α-helix | 153-158 | 6 | |
| α-helix | 161-168 | 8 | |
| α-helix | 174-190 | 17 | |
| α-helix | 203-210 | 8 | |
| α-helix | 219-226 | 8 | |
| α-helix | 234-244 | 11 | |
| α-helix | 245-247 | 3 | |
| α-helix | 253-266 | 14 | |
| α-helix | 274-289 | 16 | |
| α-helix | 296-312 | 17 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-324 | 6 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-345 | 14 | |
| α-helix | 351-363 | 13 | |
| α-helix | 367-383 | 17 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-399 | 12 | |
| α-helix | 404-418 | 15 | |
| α-helix | 426-432 | 7 | |
| α-helix | 442-453 | 12 | |
| α-helix | 456-458 | 3 | |
| α-helix | 462-470 | 9 | |
| α-helix | 478-494 | 17 | |
| α-helix | 500-508 | 9 | |
| α-helix | 509-513 | 5 | |
| α-helix | 517-532 | 16 | |
| α-helix | 534-541 | 8 | |
| α-helix | 547-549 | 3 | |
| α-helix | 557-564 | 8 | |
| β-strand | 569 | 1 | 3 |
| α-helix | 570-572 | 3 | |
| α-helix | 578-580 | 3 | |
Chains I and S: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 5 |
| β-strand | 14-19 | 6 | 5 |
| α-helix | 25-39 | 15 | |
| β-strand | 49-52 | 4 | 5 |
| β-strand | 55-62 | 8 | 5 |
| β-strand | 65-71 | 7 | 5 |
| α-helix | 77-91 | 15 | |
| α-helix | 92-96 | 5 | |
| β-strand | 99 | 1 | 6 |
| α-helix | 102-105 | 4 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 7 |
| β-strand | 122-123 | 2 | 7 |
| α-helix | 128-135 | 8 | |
Chain L: 36 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-20 | 10 | |
| α-helix | 28-40 | 13 | |
| α-helix | 52-66 | 15 | |
| α-helix | 76-82 | 7 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 188-193 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 201-214 | 14 | |
| α-helix | 225-238 | 14 | |
| β-strand | 248-249 | 2 | 8 |
| β-strand | 252-253 | 2 | 8 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-292 | 19 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-339 | 16 | |
| α-helix | 344-356 | 13 | |
| α-helix | 365-369 | 5 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-394 | 12 | |
| α-helix | 402-414 | 13 | |
| α-helix | 418-435 | 18 | |
| α-helix | 439-449 | 11 | |
| α-helix | 454-456 | 3 | |
| α-helix | 459-471 | 13 | |
| α-helix | 476-486 | 11 | |
| α-helix | 494-506 | 13 | |
| α-helix | 515-517 | 3 | |
| α-helix | 519-530 | 12 | |
| α-helix | 535-551 | 17 | |
| α-helix | 556-560 | 5 | |
| α-helix | 566-569 | 4 | |
| α-helix | 574-588 | 15 | |
| α-helix | 592-598 | 7 | |
| β-strand | 611-614 | 4 | 9 |
Chains M and U: 11 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 10 |
| β-strand | 14-19 | 6 | 10 |
| α-helix | 27-32 | 6 | |
| α-helix | 33-37 | 5 | |
| β-strand | 47-49 | 3 | 10 |
| β-strand | 54-59 | 6 | 10 |
| β-strand | 64-69 | 6 | 10 |
| β-strand | 74 | 1 | 3 |
| α-helix | 75-93 | 19 | |
| α-helix | 98-102 | 5 | |
| α-helix | 105-115 | 11 | |
| β-strand | 116-117 | 2 | 11 |
| β-strand | 120-121 | 2 | 11 |
| α-helix | 129-131 | 3 | |
| β-strand | 171-185 | 15 | 12 |
| β-strand | 191-197 | 7 | 12 |
| β-strand | 200-205 | 6 | 12 |
| β-strand | 211-216 | 6 | 13 |
| β-strand | 245-248 | 4 | 12 |
| β-strand | 252-253 | 2 | 13 |
| α-helix | 254-256 | 3 | |
| β-strand | 263-265 | 3 | 13 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-279 | 10 | 12 |
| β-strand | 287-292 | 6 | 2 |
| β-strand | 302-309 | 8 | 2 |
| β-strand | 316-325 | 10 | 12 |
| α-helix | 326-327 | 2 | |
| β-strand | 330-335 | 6 | 2 |
| β-strand | 341-345 | 5 | 12 |
| α-helix | 346-348 | 3 | |
| β-strand | 350-359 | 10 | 12 |
| β-strand | 363-372 | 10 | 2 |
| β-strand | 386-392 | 7 | 12 |
| β-strand | 401-407 | 7 | 13 |
| α-helix | 415-417 | 3 | |
| β-strand | 418-433 | 16 | 12 |
Chains P and Q: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7 | 1 | 14 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ap-2 complex subunit alpha-2 | A, L | protein | 623 | MUS MUSCULUS | P17427 (AlphaFold model) |
| Ap-2 complex subunit beta-1 | B, E | protein | 591 | HOMO SAPIENS | P63010 (AlphaFold model) |
| Ap-2 complex subunit sigma-1 | I, S | protein | 142 | MUS MUSCULUS | P62743 (AlphaFold model) |
| Ap-2 complex subunit mu-1 | M, U | protein | 435 | RATTUS NORVEGICUS | P84092 (AlphaFold model) |
| CD4 peptide | P, Q | protein | 11 | HOMO SAPIENS | P01730 |
Sequence of entity 1 (A, L), FASTA
>2JKT_1 AP-2 COMPLEX SUBUNIT ALPHA-2 (chains A, L)
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC
KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL
ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP
DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA
STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV
QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE
FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI
REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA
KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL
LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE
EMPPFPERESSILAKLKKKKGGS
Sequence of entity 2 (B, E), FASTA
>2JKT_2 AP-2 COMPLEX SUBUNIT BETA-1 (chains B, E)
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT
DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE
YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA
VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI
CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY
VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE
YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK
YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV
QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV
VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK
Sequence of entity 3 (I, S), FASTA
>2JKT_3 AP-2 COMPLEX SUBUNIT SIGMA-1 (chains I, S)
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR
RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA
GEIRETSQTKVLKQLLMLQSLE
Sequence of entity 4 (M, U), FASTA
>2JKT_4 AP-2 COMPLEX SUBUNIT MU-1 (chains M, U)
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR
SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY
PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES
VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS
IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK
LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG
MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK
WVRYIGRSGIYETRC
Sequence of entity 5 (P, Q), FASTA
>2JKT_5 CD4 PEPTIDE (chains P, Q)
RMSEIKRLLSE
Primary citation
A Structural Explanation for the Binding of Endocytic Dileucine Motifs by the Ap2 Complex. Kelly, B.T., Mccoy, A.J., Spaete, K. et al. Nature (2008) 456:976. DOI 10.1038/NATURE07422 · PubMed
Other PDB entries of the same protein (UniProt P17427 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1KYF 1.22 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
- 1QTS 1.4 Å, Crystal structure of the ap-2 clathrin adaptor alpha-appendage
- 7OHI 1.41 Å, FCHO1-peptide-AP2 alpha ear complex
- 1QTP 1.6 Å, Crystal structure of the ap-2 clathrin adaptor alpha-appendage
- 2VJ0 1.6 Å, Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex,…
- 1KYU 1.8 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
- 1B9K 1.9 Å, Alpha-adaptin appendage domain, from clathrin adaptor AP2
- 1W80 1.9 Å, Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex,…
- 3HS8 1.9 Å, Intersectin 1-peptide-AP2 alpha ear complex
- 9PUE 1.91 Å, Structure of Alpha Appendage of AP2 bound to the FxDxF motif derived of CCDC32
- 1KY6 2.0 Å, Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide
- 1KYD 2.0 Å, Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide
Browse structure collections
About this viewer
MolViewer shows 2JKT 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.