7RWB: AP2

AP2 bound to the APA domain of SGIP in the presence of heparin. Determined by electron microscopy at 3.9 Å resolution. Released 30 Mar 2022.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Mus musculus
Chains: 8
Atoms: 23,962
Mol. weight: 408.58 kDa
Released: 30 Mar 2022

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

Secondary structure: helices and β-sheets

7RWB contains 192 α-helices and 70 β-strands across 8 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.

Chains a and A: 44 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	12-21	10
α-helix	26-44	19
α-helix	52-68	17
α-helix	77-80	4
α-helix	88-100	13
α-helix	106-120	15
α-helix	125-138	14
α-helix	141-147	7
α-helix	151-155	5
α-helix	162-178	17
α-helix	180-182	3
α-helix	189-195	7
α-helix	202-217	16
α-helix	219-222	4
α-helix	225-237	13
α-helix	245-247	3
β-strand	248-249	2	11
β-strand	252-253	2	11
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	360-362	3
α-helix	363-367	5
α-helix	370-379	10
α-helix	384-395	12
α-helix	402-415	14
α-helix	418-420	3
α-helix	421-434	14
α-helix	439-452	14
α-helix	461-472	12
α-helix	476-487	12
α-helix	494-507	14
α-helix	515-517	3
α-helix	519-530	12
α-helix	535-551	17
α-helix	553-555	3
α-helix	556-563	8
α-helix	566-569	4
α-helix	574-589	16
α-helix	595-598	4
α-helix	603-606	4
α-helix	611-619	9

Chains b and B: 36 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	27-43	17
α-helix	48-50	3
α-helix	51-57	7
α-helix	63-77	15
α-helix	82-87	6
α-helix	88-95	8
α-helix	100-111	12
α-helix	118-128	11
α-helix	135-150	16
α-helix	156-169	14
α-helix	174-187	14
α-helix	203-212	10
α-helix	216-226	11
α-helix	234-243	10
α-helix	253-265	13
α-helix	277-290	14
α-helix	296-312	17
α-helix	321-324	4
α-helix	332-344	13
α-helix	351-361	11
α-helix	367-383	17
α-helix	388-399	12
α-helix	404-418	15
α-helix	426-428	3
α-helix	429-434	6
α-helix	442-454	13
α-helix	462-469	8
α-helix	478-494	17
α-helix	503-512	10
α-helix	517-530	14
α-helix	534-540	7
α-helix	545-547	3
α-helix	554-556	3
α-helix	557-564	8
β-strand	569	1	12
α-helix	570-574	5
α-helix	578-580	3

Chains m and M: 11 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	13
β-strand	14-18	5	13
α-helix	26-32	7
α-helix	33-37	5
α-helix	42-44	3
β-strand	47	1	13
β-strand	50	1	14
β-strand	53	1	14
β-strand	54-60	7	13
β-strand	63-69	7	13
β-strand	74	1	12
α-helix	75-93	19
α-helix	98-103	6
α-helix	105-115	11
β-strand	116-117	2	15
β-strand	120-121	2	15
α-helix	126-132	7
β-strand	172-185	14	16
β-strand	191-205	15	16
β-strand	211-216	6	17
β-strand	263-265	3	17
α-helix	267-268	2
β-strand	270-279	10	16
β-strand	287-294	8	18
β-strand	300-309	10	18
β-strand	316-325	10	16
β-strand	330-337	8	18
β-strand	341-345	5	16
β-strand	350-359	10	16
β-strand	363-372	10	18
α-helix	380-382	3
α-helix	384-385	2
β-strand	386-392	7	16
β-strand	401-407	7	17
α-helix	415-417	3
β-strand	419-433	15	16

Chains s and S: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	19
β-strand	14-19	6	19
α-helix	25-41	17
β-strand	49-52	4	19
β-strand	55-62	8	19
β-strand	65-71	7	19
α-helix	78-95	18
α-helix	100-105	6
α-helix	107-117	11
β-strand	119	1	20
β-strand	122	1	20
α-helix	129-137	9

Molecules and chains

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

Sequence of entity 1 (A, a), FASTA

>7RWB_1 AP-2 complex subunit alpha-2 (chains A, a)
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVC
KLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDL
ASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSP
DLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSA
STDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKV
QHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSE
FSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSI
REEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAA
KTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRAL
LLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLE
EMPPFPERESSILAKLKKKKGGSGLEVLFQ

Sequence of entity 2 (B, b), FASTA

>7RWB_2 AP-2 complex subunit beta (chains B, b)
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQT
DNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITE
YLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANA
VAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSI
CERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQY
VALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKE
YATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRK
YPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQV
QLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEV
VLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRK

Sequence of entity 3 (M, m), FASTA

>7RWB_3 AP-2 complex subunit mu (chains M, m)
MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKR
SNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGY
PQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLES
VNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQS
IAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTK
LEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAG
MKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIK
WVRYIGRSGIYETRC

Sequence of entity 4 (S, s), FASTA

>7RWB_4 AP-2 complex subunit sigma (chains S, 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

Browse structure collections

About this viewer

MolViewer shows 7RWB 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.