4K17: Mouse CARMIL residues 1-668

Crystal Structure of mouse CARMIL residues 1-668. Determined by X-ray diffraction at 2.9 Å resolution. Released 9 Oct 2013.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Mus musculus
Chains: 4
Atoms: 20,371
Mol. weight: 299.39 kDa
Ligands: OHB, ABU
Released: 9 Oct 2013

Explore 4K17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K17 contains 132 α-helices and 108 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: 33 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	11-17	7
β-strand	28-36	9	1
β-strand	40-48	9	1
β-strand	52-57	6	1
β-strand	66-69	4	1
β-strand	73-77	5	1
β-strand	83-88	6	1
β-strand	93-97	5	1
α-helix	100-116	17
α-helix	123-126	4
β-strand	129-131	3	1
α-helix	135-147	13
α-helix	151-153	3
α-helix	155-170	16
α-helix	176-180	5
α-helix	181-186	6
α-helix	187-189	3
β-strand	193-195	3	2
α-helix	196-199	4
α-helix	205-207	3
α-helix	208-212	5
β-strand	222-226	5	2
α-helix	229-231	3
α-helix	232-244	13
β-strand	250-254	5	2
β-strand	259	1	3
α-helix	260-272	13
β-strand	280-282	3	2
β-strand	287	1	3
α-helix	291-301	11
β-strand	309-311	3	2
α-helix	319-331	13
α-helix	335-338	4
β-strand	341-343	3	2
α-helix	355-362	8
β-strand	369-371	3	2
β-strand	378	1	4
α-helix	379-389	11
β-strand	396-398	3	2
β-strand	403	1	4
α-helix	414-422	9
β-strand	428-430	3	2
α-helix	438-449	12
β-strand	457-460	4	2
α-helix	466-472	7
β-strand	488-492	5	2
α-helix	499-501	3
α-helix	502-510	9
β-strand	517-519	3	2
α-helix	529-544	16
β-strand	552-554	3	2
α-helix	561-564	4
α-helix	565-568	4
α-helix	570-573	4
β-strand	579-581	3	2
α-helix	588-601	14
β-strand	607-609	3	2
α-helix	617-628	12
β-strand	635	1	2
α-helix	640-649	10
α-helix	651-667	17

Chain B: 33 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	10-20	11
β-strand	26-34	9	5
β-strand	42-49	8	5
β-strand	52-57	6	5
β-strand	64-69	6	5
α-helix	70-72	3
β-strand	75-78	4	5
β-strand	83-87	5	5
β-strand	92-96	5	5
α-helix	100-116	17
α-helix	123-126	4
β-strand	130-132	3	5
α-helix	135-147	13
α-helix	150-152	3
α-helix	155-170	16
α-helix	176-181	6
α-helix	182-187	6
β-strand	193-195	3	6
α-helix	196-199	4
α-helix	205-207	3
α-helix	208-212	5
β-strand	222-226	5	6
α-helix	229-231	3
α-helix	232-244	13
β-strand	250-254	5	6
β-strand	259	1	7
α-helix	260-272	13
β-strand	280-282	3	6
β-strand	287	1	7
α-helix	289-301	13
β-strand	309-311	3	6
α-helix	319-331	13
α-helix	335-338	4
β-strand	341-343	3	6
α-helix	355-362	8
β-strand	369-371	3	6
β-strand	378	1	8
α-helix	379-389	11
β-strand	396-398	3	6
β-strand	403	1	8
α-helix	414-422	9
β-strand	428-430	3	6
α-helix	438-449	12
β-strand	457-460	4	6
α-helix	466-470	5
β-strand	488-492	5	6
α-helix	499-501	3
α-helix	502-510	9
β-strand	517-519	3	6
α-helix	529-544	16
β-strand	552-554	3	6
α-helix	561-564	4
α-helix	565-568	4
α-helix	569-572	4
β-strand	579-581	3	6
α-helix	588-601	14
β-strand	607-609	3	6
α-helix	617-628	12
β-strand	635	1	6
α-helix	640-646	7
α-helix	651-667	17

Chain C: 33 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	13-20	8
β-strand	28-35	8	9
β-strand	41-48	8	9
β-strand	52-57	6	9
β-strand	64-69	6	9
α-helix	70-72	3
β-strand	73-78	6	9
β-strand	83-88	6	9
β-strand	92-97	6	9
α-helix	100-116	17
α-helix	123-126	4
β-strand	129-132	4	9
α-helix	136-147	12
α-helix	152-154	3
α-helix	155-170	16
α-helix	176-180	5
α-helix	181-186	6
α-helix	187-189	3
β-strand	193-195	3	10
α-helix	196-199	4
α-helix	204-206	3
α-helix	207-212	6
β-strand	222-226	5	10
α-helix	229-231	3
α-helix	232-244	13
β-strand	250-254	5	10
α-helix	260-272	13
β-strand	280-282	3	10
α-helix	290-301	12
β-strand	309-311	3	10
α-helix	319-331	13
α-helix	335-338	4
β-strand	341-343	3	10
α-helix	355-362	8
β-strand	369-371	3	10
β-strand	378	1	11
α-helix	379-389	11
β-strand	396-398	3	10
β-strand	403	1	11
α-helix	414-422	9
β-strand	428-430	3	10
α-helix	438-450	13
β-strand	457-460	4	10
α-helix	466-471	6
β-strand	488-492	5	10
α-helix	499-501	3
α-helix	502-511	10
β-strand	517-519	3	10
α-helix	529-544	16
β-strand	552-554	3	10
α-helix	565-568	4
α-helix	569-572	4
β-strand	579-581	3	10
α-helix	588-601	14
β-strand	607-609	3	10
α-helix	617-628	12
β-strand	635	1	10
α-helix	640-649	10
α-helix	651-667	17

Chain D: 33 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	11-20	10
β-strand	28-34	7	12
β-strand	42-48	7	12
β-strand	52-57	6	12
α-helix	62	1
β-strand	64-69	6	12
β-strand	73-78	6	12
β-strand	83-88	6	12
β-strand	92-97	6	12
α-helix	100-116	17
α-helix	123-127	5
β-strand	129-132	4	12
α-helix	135-147	13
α-helix	150-152	3
α-helix	155-170	16
α-helix	176-180	5
α-helix	181-185	5
α-helix	186-188	3
β-strand	193-195	3	13
α-helix	196-199	4
α-helix	207-212	6
β-strand	222-226	5	13
α-helix	229-231	3
α-helix	232-244	13
β-strand	250-254	5	13
α-helix	260-272	13
β-strand	280-282	3	13
α-helix	290-301	12
β-strand	309-311	3	13
α-helix	319-331	13
α-helix	335-338	4
β-strand	341-343	3	13
α-helix	355-362	8
β-strand	369-371	3	13
β-strand	378	1	14
α-helix	379-389	11
β-strand	396-398	3	13
β-strand	403	1	14
α-helix	414-422	9
β-strand	428-430	3	13
α-helix	438-449	12
β-strand	457-460	4	13
α-helix	466-472	7
β-strand	488-492	5	13
α-helix	499-501	3
α-helix	502-510	9
β-strand	517-519	3	13
α-helix	529-544	16
β-strand	552-554	3	13
α-helix	561-564	4
α-helix	565-568	4
α-helix	569-572	4
β-strand	579-581	3	13
α-helix	588-601	14
β-strand	607-609	3	13
α-helix	617-628	12
β-strand	635	1	13
α-helix	640-649	10
α-helix	651-667	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leucine-rich repeat-containing protein 16A	A, B, C, D	protein	669	Mus musculus	Q6EDY6 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4K17_1 Leucine-rich repeat-containing protein 16A (chains A, B, C, D)
SMTDESSDVPRELMESIKDVIGRKIKISVKKKVKLEVKGDRVENKVLVLTSCRAFLLSAR
IPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRIFP
GLSPLRIMKKVSMEPSERLASLQALWDSQTLAEPGPCGGFSQMYACVCDWLGFSYKEEVQ
WDVDTIYLTQDTRELNLQDFSHLEHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQIL
RVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQ
FAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPLTASTLTHLDLSGNALRGDDLSHMYN
FLAQPNTIVHLDLSNTECSLEMVCSALLRGCLQCLAVLNLSRSVFSHRKGKEVPPSFKQF
FSSSLALIQINLSGTKLSPEPLKALLLGLACNHSLKGVSLDLSNCELGHCLRSGGAQVLE
GCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNL
VQMIQDEDSPLQSLSLADSKLKAEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKAL
QINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDAAQALKTNPEKTEEALQ
KIENYLLRN

Ligands and cofactors

ID	Name	Formula	Copies
OHB	salicylamide	C7 H7 N O2	1
ABU	Gamma-amino-butanoic acid	C4 H9 N O2	1

Water and common crystallization additives (CL) are not listed.

Primary citation

CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Zwolak, A., Yang, C., Feeser, E.A. et al. Nat Commun (2013) 4:2523-2523. DOI 10.1038/ncomms3523 · PubMed

Other PDB entries of the same protein (UniProt Q6EDY6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3AA0 1.7 Å, Crystal structure of Actin Capping Protein in complex with the Cp-binding motif derived…
3AAE 3.3 Å, Crystal structure of Actin capping protein in complex with CARMIL fragment
2KZ7 Solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP)

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