2XA7: PDB entry 2XA7

AP2 clathrin adaptor core in active complex with cargo peptides. Determined by X-ray diffraction at 3.1 Å resolution. Released 21 Jul 2010.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: RATTUS NORVEGICUS, HOMO SAPIENS, MUS MUSCULUS
Chains: 5
Atoms: 14,137
Mol. weight: 206.12 kDa
Released: 21 Jul 2010

Explore 2XA7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2XA7 contains 93 α-helices and 35 β-strands across 5 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: 38 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	11-21	11
α-helix	26-44	19
α-helix	52-69	18
α-helix	77-80	4
α-helix	88-100	13
α-helix	107-120	14
α-helix	125-137	13
α-helix	141-146	6
α-helix	151-155	5
α-helix	162-178	17
α-helix	189-192	4
α-helix	201-217	17
α-helix	219-222	4
α-helix	225-237	13
α-helix	245-247	3
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	324-337	14
α-helix	343-356	14
α-helix	360-362	3
α-helix	363-367	5
α-helix	370-379	10
α-helix	383-396	14
α-helix	399-414	16
α-helix	419-435	17
α-helix	440-452	13
α-helix	460-472	13
α-helix	476-487	12
α-helix	495-511	17
α-helix	519-530	12
α-helix	535-550	16
α-helix	553-555	3
α-helix	557-564	8
α-helix	566-569	4
α-helix	574-588	15
α-helix	593-598	6
α-helix	611-619	9

Chain B: 40 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-22	9
α-helix	27-43	17
α-helix	48-50	3
α-helix	51-58	8
α-helix	63-77	15
α-helix	81-84	4
α-helix	85-87	3
α-helix	88-94	7
α-helix	100-110	11
α-helix	118-127	10
α-helix	135-149	15
α-helix	157-169	13
α-helix	174-187	14
α-helix	201-213	13
α-helix	216-226	11
α-helix	235-244	10
α-helix	253-265	13
α-helix	276-283	8
α-helix	285-290	6
α-helix	296-312	17
α-helix	320-324	5
α-helix	325-327	3
α-helix	332-345	14
α-helix	351-361	11
α-helix	367-383	17
α-helix	385-399	15
α-helix	404-420	17
α-helix	425-428	4
α-helix	429-434	6
α-helix	442-454	13
α-helix	462-469	8
α-helix	478-494	17
α-helix	496-498	3
α-helix	500-512	13
α-helix	517-527	11
α-helix	534-540	7
α-helix	557-564	8
β-strand	569	1	2
α-helix	570	1
α-helix	571-575	5
α-helix	578-580	3

Chain M: 10 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	3
β-strand	14-17	4	3
α-helix	26-35	10
β-strand	47-50	4	3
β-strand	53-60	8	3
β-strand	63-69	7	3
β-strand	74	1	2
α-helix	75-93	19
α-helix	98-102	5
α-helix	105-114	10
β-strand	116-117	2	4
β-strand	120-121	2	4
α-helix	129-131	3
α-helix	145-156	12
β-strand	172-185	14	5
β-strand	191-204	14	5
β-strand	211-215	5	6
β-strand	256-259	4	5
α-helix	265-271	7
β-strand	274-276	3	6
α-helix	278-279	2
β-strand	281-290	10	5
α-helix	294-296	3
β-strand	300-307	8	7
β-strand	311-319	9	7
β-strand	327-335	9	5
β-strand	345-348	4	7
β-strand	352-356	5	5
β-strand	361-370	10	5
β-strand	374-382	9	7
β-strand	397-403	7	5
β-strand	414-418	5	6
α-helix	426-428	3
β-strand	430-444	15	5

Chain P: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	3-4	2	5

Chain S: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	8
β-strand	14-19	6	8
α-helix	26-39	14
β-strand	49-52	4	8
β-strand	55-62	8	8
β-strand	65-71	7	8
α-helix	77-94	18
α-helix	100-105	6
α-helix	107-117	11
β-strand	118-119	2	9
β-strand	122-123	2	9
α-helix	128-137	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adaptor-related protein complex 2, alpha 2 subunit	A	protein	621	RATTUS NORVEGICUS	P18484 (AlphaFold model)
Ap-2 complex subunit beta	B	protein	592	HOMO SAPIENS	P63010 (AlphaFold model)
Ap-2 complex subunit mu,	M	protein	446	RATTUS NORVEGICUS	P84092 (AlphaFold model)
TGN38 cargo peptide	P	protein	6	HOMO SAPIENS
Ap-2 complex subunit sigma	S	protein	142	MUS MUSCULUS	P62743 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2XA7_1 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA 2 SUBUNIT (chains A)
MPAVSKGEGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC
KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL
ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP
DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA
STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV
QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE
FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI
REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA
KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL
LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE
EMPPFPERESSILAKLKKKKG

Sequence of entity 2 (B), FASTA

>2XA7_2 AP-2 COMPLEX SUBUNIT BETA (chains B)
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT
DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE
YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA
VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI
CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY
VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE
YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK
YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV
QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV
VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKH

Sequence of entity 3 (M), FASTA

>2XA7_3 AP-2 COMPLEX SUBUNIT MU, (chains M)
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR
SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY
PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES
VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSMEQK
LISEEDLGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRV
IPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASEN
AIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEP
KLNYSDHDVIKWVRYIGRSGIYETRC

Sequence of entity 4 (P), FASTA

>2XA7_4 TGN38 CARGO PEPTIDE (chains P)
DYQRLN

Sequence of entity 5 (S), FASTA

>2XA7_5 AP-2 COMPLEX SUBUNIT SIGMA (chains S)
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR
RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA
GEIRETSQTKVLKQLLMLQSLE

Primary citation

A Large Scale Conformational Change Couples Membrane Recruitment to Cargo Binding in the Ap2 Clathrin Adaptor Complex. Jackson, L.P., Kelly, B.T., Mccoy, A.J. et al. Cell (2010) 141:1241. DOI 10.1016/J.CELL.2010.05.005 · PubMed

Other PDB entries of the same protein (UniProt P18484 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QH5 2.56 Å, AP2 clathrin adaptor mu2T156-phosphorylated core in closed conformation
2VGL 2.6 Å, AP2 clathrin adaptor core
4UQI 2.79 Å, AP2 controls clathrin polymerization with a membrane-activated switch
7OHO 2.88 Å, Crystal structure of AP2 FCHO2 chimera
4NEE 2.88 Å, crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef
6URI 3.0 Å, HIV-1 Nef in complex with the CD4 cytoplasmic domain and the AP2 clathrin adaptor complex
7OG1 3.25 Å, AP2 clathrin adaptor core in complex with cargo peptide and FCHO2
6QH7 3.4 Å, AP2 clathrin adaptor mu2T156-phosphorylated core with two cargo peptides in open+…
6OWT 3.8 Å, Structure of SIVsmm Nef and SMM tetherin bound to the clathrin adaptor AP-2 complex
6YAE 3.9 Å, AP2 core in physiological buffer
7Z5C 4.16 Å, Chimera of AP2 with FCHO2 linker domain as a fusion on Cmu2 subunit
6QH6 5.0 Å, AP2 clathrin adaptor core with two cargo peptides in open+ conformation

Browse structure collections

About this viewer

MolViewer shows 2XA7 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.