6M3P: AnkG/beta2-spectrin complex

Crystal structure of AnkG/beta2-spectrin complex. Determined by X-ray diffraction at 3.31 Å resolution. Released 13 May 2020.

Method: X-ray diffraction
Resolution: 3.31 Å
Organisms: Rattus norvegicus, Mus musculus
Chains: 4
Atoms: 10,198
Mol. weight: 183.25 kDa
Released: 13 May 2020

Explore 6M3P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M3P contains 40 α-helices and 71 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: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	12-25	14
α-helix	34-66	33
α-helix	76-132	57
α-helix	140-178	39
α-helix	185-237	53
α-helix	248-254	7
α-helix	255-259	5
α-helix	260-283	24
α-helix	287-311	25

Chain B: 9 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	12-25	14
α-helix	34-66	33
α-helix	76-132	57
α-helix	140-178	39
α-helix	185-237	53
α-helix	248-254	7
α-helix	255-259	5
α-helix	260-283	24
α-helix	287-311	25
β-strand	316-317	2	6

Chain C: 11 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	964-968	5	9
β-strand	971-974	4	10
β-strand	979-983	5	9
β-strand	990-993	4	9
β-strand	1002-1005	4	10
β-strand	1006-1008	3	11
α-helix	1013-1014	2
β-strand	1025-1033	9	11
β-strand	1039-1049	11	9
β-strand	1052	1	12
β-strand	1059-1066	8	11
β-strand	1072-1074	3	11
α-helix	1082-1086	5
α-helix	1098-1104	7
β-strand	1106-1113	8	9
β-strand	1117-1124	8	11
β-strand	1127-1129	3	13
β-strand	1138-1139	2	14
β-strand	1147-1149	3	14
β-strand	1161-1166	6	13
α-helix	1170-1175	6
β-strand	1182-1183	2	13
β-strand	1186-1189	4	13
β-strand	1195-1205	11	14
α-helix	1206-1209	4
β-strand	1225-1230	6	13
α-helix	1237-1238	2
β-strand	1241-1242	2	13
α-helix	1244-1246	3
β-strand	1250	1	14
β-strand	1255-1262	8	14
β-strand	1265-1270	6	13
α-helix	1274-1288	15
α-helix	1290-1291	2
β-strand	1292-1295	4	12
β-strand	1296-1301	6	15
β-strand	1311-1316	6	15
α-helix	1319-1320	2
α-helix	1324-1328	5
β-strand	1332-1336	5	15
β-strand	1340-1343	4	12
β-strand	1347-1353	7	16
β-strand	1367-1369	3	16
β-strand	1376-1380	5	15
β-strand	1393-1398	6	16
β-strand	1413-1417	5	16

Chain E: 11 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	964-968	5	1
β-strand	971-974	4	2
β-strand	979-983	5	1
β-strand	990-993	4	1
β-strand	1002-1005	4	2
β-strand	1006-1008	3	3
α-helix	1013-1014	2
β-strand	1025-1033	9	3
β-strand	1039-1049	11	1
β-strand	1052	1	4
β-strand	1059-1066	8	3
β-strand	1072-1074	3	3
α-helix	1082-1086	5
α-helix	1098-1104	7
β-strand	1106-1113	8	1
β-strand	1117-1124	8	3
β-strand	1127-1129	3	5
β-strand	1138-1139	2	6
β-strand	1147-1149	3	6
β-strand	1161-1166	6	5
α-helix	1170-1175	6
β-strand	1182-1183	2	5
β-strand	1186-1189	4	5
β-strand	1194-1205	12	6
α-helix	1206-1209	4
β-strand	1225-1230	6	5
α-helix	1237-1238	2
β-strand	1241-1242	2	5
α-helix	1244-1246	3
β-strand	1250	1	6
β-strand	1255-1262	8	6
β-strand	1265-1270	6	5
α-helix	1276-1288	13
α-helix	1290-1291	2
β-strand	1292-1295	4	4
β-strand	1296-1301	6	7
β-strand	1311-1316	6	7
α-helix	1319-1320	2
α-helix	1324-1328	5
β-strand	1332-1335	4	7
β-strand	1340-1343	4	4
β-strand	1347-1353	7	8
β-strand	1367-1369	3	8
β-strand	1376-1380	5	7
β-strand	1393-1398	6	8
β-strand	1413-1417	5	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ankyrin-3	C, E	protein	491	Rattus norvegicus	O70511 (AlphaFold model)
Spectrin beta chain, non-erythrocytic 1	A, B	protein	320	Mus musculus	Q62261 (AlphaFold model)

Sequence of entity 1 (C, E), FASTA

>6M3P_1 Ankyrin-3 (chains C, E)
ADTLDNVNLVSSPVHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVK
RHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGE
TWKEHQFDSKNEDLSELLNGMDEELDSPEELGTKRICRIITKDFPQYFAVVSRIKQESNQ
IGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPEETVKKILGNKATFSPIVTVE
PRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPSLRLLCSITGGTSPAQWEDITGTTPL
TFIKDCVSFTTNVSARFWLADCHQVLETVGLASQLYRELICVPYMAKFVVFAKTNDPVES
SLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFN
FYSFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKAEKAD
RRQSFTSLALR

Sequence of entity 2 (A, B), FASTA

>6M3P_2 Spectrin beta chain, non-erythrocytic 1 (chains A, B)
AHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQ
LSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDL
EQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNNMADELINSGH
SDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPE
ELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVL
EAWKSLLDACEGRRVRLVDT

Primary citation

Structural Basis Underlying Strong Interactions between Ankyrins and Spectrins. Li, J., Chen, K., Zhu, R. et al. J Mol Biol (2020) 432:3838-3850. DOI 10.1016/j.jmb.2020.04.023 · PubMed

Other PDB entries of the same protein (UniProt O70511 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5YIP 1.85 Å, Crystal Structure of AnkG LIR/GABARAPL1 complex
6A9X 2.2 Å, Crystal Structure of AnkG/GABARAP Complex
7XCE 2.5 Å, Crystal structure of Ankyrin G in complex with neurofascin
5YIQ 2.6 Å, Crystal structure of AnkG LIR/LC3B complex
6M3R 4.31 Å, Crystal structure of AnkG/beta4-spectrin complex

Browse structure collections

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