7RW8: AP2

AP2 bound to heparin in the closed conformation. Determined by electron microscopy at 3.5 Å resolution. Released 30 Mar 2022.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Mus musculus
Chains: 4
Atoms: 12,572
Mol. weight: 204.29 kDa
Released: 30 Mar 2022

Explore 7RW8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7RW8 contains 98 α-helices and 36 β-strands across 4 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: 43 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	11-21	11
α-helix	26-45	20
α-helix	52-68	17
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	151-156	6
α-helix	162-178	17
α-helix	180-182	3
α-helix	189-194	6
α-helix	195-197	3
α-helix	201-215	15
α-helix	219-222	4
α-helix	223-225	3
α-helix	226-237	12
β-strand	248	1	1
β-strand	253	1	1
α-helix	255-266	12
α-helix	269-271	3
α-helix	274-292	19
α-helix	294-295	2
α-helix	300-320	21
α-helix	324-337	14
α-helix	343-356	14
α-helix	363-368	6
α-helix	370-378	9
α-helix	383-395	13
α-helix	402-415	14
α-helix	418-434	17
α-helix	439-453	15
α-helix	454-456	3
α-helix	461-471	11
α-helix	476-486	11
α-helix	494-507	14
α-helix	508-510	3
α-helix	515-517	3
α-helix	519-530	12
α-helix	535-551	17
α-helix	556-563	8
α-helix	566-569	4
α-helix	574-588	15
α-helix	592-598	7
α-helix	603-605	3

Chain B: 41 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-22	9
α-helix	27-42	16
α-helix	48-50	3
α-helix	51-57	7
α-helix	63-79	17
α-helix	81-85	5
α-helix	88-91	4
α-helix	92-94	3
α-helix	100-111	12
α-helix	117-121	5
α-helix	123-127	5
α-helix	135-150	16
α-helix	158-169	12
α-helix	177-188	12
α-helix	200-211	12
α-helix	216-227	12
α-helix	234-244	11
α-helix	254-265	12
α-helix	277-283	7
α-helix	285-291	7
α-helix	296-312	17
α-helix	321-324	4
α-helix	325-327	3
α-helix	332-344	13
α-helix	351-361	11
α-helix	367-383	17
α-helix	388-400	13
α-helix	404-420	17
α-helix	426-428	3
α-helix	429-434	6
α-helix	442-453	12
α-helix	462-470	9
α-helix	478-494	17
α-helix	500-508	9
α-helix	509-513	5
α-helix	517-530	14
α-helix	534-541	8
α-helix	543-547	5
α-helix	557-565	9
β-strand	569	1	2
α-helix	571-574	4
α-helix	578-580	3

Chain M: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	3
β-strand	14-19	6	3
α-helix	26-32	7
α-helix	33-37	5
α-helix	42-44	3
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	98-103	6
α-helix	105-115	11
β-strand	116-117	2	4
β-strand	120-121	2	4
α-helix	129-132	4
β-strand	172-185	14	5
β-strand	191-205	15	5
β-strand	211-216	6	6
β-strand	245-248	4	5
β-strand	253-254	2	6
β-strand	262-265	4	6
α-helix	267-268	2
β-strand	270-279	10	5
β-strand	287-294	8	7
β-strand	300-309	10	7
β-strand	316-325	10	5
β-strand	330-337	8	7
β-strand	341-345	5	5
β-strand	350-359	10	5
β-strand	363-372	10	7
α-helix	382-385	4
β-strand	386-392	7	5
β-strand	401-407	7	6
β-strand	414	1	6
β-strand	419-433	15	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	25-41	17
β-strand	49-52	4	8
β-strand	55-62	8	8
β-strand	65-71	7	8
α-helix	78-95	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	128-140	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AP-2 complex subunit alpha-2	A	protein	630	Mus musculus	P17427 (AlphaFold model)
AP-2 complex subunit beta	B	protein	591	Mus musculus	Q9DBG3 (AlphaFold model)
AP-2 complex subunit mu	M	protein	435	Mus musculus	P84091 (AlphaFold model)
AP-2 complex subunit sigma	S	protein	142	Mus musculus	P62743 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7RW8_1 AP-2 complex subunit alpha-2 (chains A)
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC
KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL
ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP
DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA
STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV
QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE
FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI
REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA
KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL
LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE
EMPPFPERESSILAKLKKKKGGSGLEVLFQ

Sequence of entity 2 (B), FASTA

>7RW8_2 AP-2 complex subunit beta (chains B)
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT
DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE
YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA
VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI
CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY
VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE
YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK
YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV
QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV
VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK

Sequence of entity 3 (M), FASTA

>7RW8_3 AP-2 complex subunit mu (chains M)
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR
SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY
PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES
VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS
IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK
LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG
MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK
WVRYIGRSGIYETRC

Sequence of entity 4 (S), FASTA

>7RW8_4 AP-2 complex subunit sigma (chains S)
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR
RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA
GEIRETSQTKVLKQLLMLQSLE

Primary citation

Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Partlow, E.A., Cannon, K.S., Hollopeter, G. et al. Nat Struct Mol Biol (2022) 29:339-347. DOI 10.1038/s41594-022-00749-z · 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

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