3LK4: CapZ

Crystal structure of CapZ bound to the uncapping motif from CD2AP. Determined by X-ray diffraction at 1.99 Å resolution. Released 7 Apr 2010.

Method: X-ray diffraction
Resolution: 1.99 Å
Organisms: Gallus gallus, homo sapiens
Chains: 36
Atoms: 54,370
Mol. weight: 811.56 kDa
Released: 7 Apr 2010

Explore 3LK4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LK4 contains 325 α-helices and 252 β-strands across 36 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 0, 3, 6, 9, C, F, I, L, O, R, U and X: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	485-487	3
α-helix	489-492	4
α-helix	494-495	2
α-helix	500-502	3

Chain 1: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	29-40	12
α-helix	43-49	7
α-helix	52-60	9
β-strand	64-65	2	6
β-strand	74-75	2	6
α-helix	78-80	3
β-strand	81	1	7
β-strand	86-89	4	7
β-strand	94-99	6	7
β-strand	104-110	7	7
α-helix	118-135	18
β-strand	140-148	9	8
β-strand	151-164	14	8
α-helix	165-167	3
β-strand	169-182	14	8
β-strand	185-198	14	8
β-strand	202-217	16	8
α-helix	221-249	29
α-helix	250-254	5
α-helix	255-258	4
α-helix	271-274	4

Chains 2, 5, B and T: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-13	9
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
β-strand	48-52	5	9
β-strand	57-61	5	9
α-helix	63-65	3
β-strand	66-67	2	10
β-strand	70-72	3	10
β-strand	79-80	2	10
α-helix	91-112	22
β-strand	116-124	9	8
β-strand	127-137	11	8
α-helix	141-143	3
β-strand	144-157	14	8
β-strand	164-179	16	8
β-strand	186-202	17	8
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6

Chains 4 and D: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	29-40	12
α-helix	43-49	7
α-helix	52-60	9
β-strand	64-65	2	16
β-strand	74-75	2	16
α-helix	78-80	3
β-strand	81	1	17
β-strand	86-89	4	17
β-strand	94-99	6	17
β-strand	104-110	7	17
α-helix	118-135	18
β-strand	139-148	10	18
β-strand	151-164	14	18
α-helix	165-167	3
β-strand	169-182	14	18
β-strand	185-198	14	18
β-strand	202-217	16	18
α-helix	221-249	29
α-helix	250-255	6
α-helix	256-258	3
α-helix	271-274	4

Chains 7 and M: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	29-40	12
α-helix	43-49	7
α-helix	51-60	10
β-strand	64-65	2	26
β-strand	74-75	2	26
α-helix	78-80	3
β-strand	81	1	27
β-strand	86-89	4	27
β-strand	94-99	6	27
β-strand	104-110	7	27
α-helix	118-135	18
β-strand	139-148	10	28
β-strand	151-164	14	28
α-helix	165-167	3
β-strand	169-182	14	28
β-strand	185-198	14	28
β-strand	202-217	16	28
α-helix	221-249	29
α-helix	250-255	6
α-helix	256-258	3
α-helix	271-274	4

Chains 8, N and W: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
β-strand	48-52	5	29
β-strand	57-61	5	29
α-helix	63-65	3
β-strand	66-67	2	30
β-strand	70-72	3	30
β-strand	79-80	2	30
α-helix	91-112	22
β-strand	116-124	9	28
β-strand	127-137	11	28
α-helix	141-143	3
β-strand	144-157	14	28
β-strand	164-179	16	28
β-strand	186-202	17	28
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6

Chain A: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	29-40	12
α-helix	43-49	7
α-helix	52-61	10
β-strand	64-65	2	1
β-strand	74-75	2	1
α-helix	78-80	3
β-strand	81	1	2
β-strand	86-89	4	2
β-strand	94-99	6	2
β-strand	104-110	7	2
α-helix	118-135	18
β-strand	139-148	10	3
β-strand	151-164	14	3
α-helix	165-167	3
β-strand	169-182	14	3
β-strand	185-198	14	3
β-strand	202-217	16	3
α-helix	221-249	29
α-helix	250-254	5
α-helix	255-258	4
α-helix	271-274	4

Chain E: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
β-strand	48-52	5	14
β-strand	57-61	5	14
α-helix	63-65	3
β-strand	66-67	2	15
β-strand	70-72	3	15
β-strand	79-80	2	15
α-helix	91-112	22
β-strand	116-124	9	13
β-strand	127-137	11	13
α-helix	141-143	3
β-strand	144-157	14	13
β-strand	164-179	16	13
β-strand	186-202	17	13
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6

6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
F-actin-capping protein subunit alpha-1	1, 4, 7, A, D, G, J, M, P, S, V, Y	protein	286	Gallus gallus	P13127 (AlphaFold model)
F-actin-capping protein subunit beta isoforms 1 and 2	2, 5, 8, B, E, H, K, N, Q, T, W, Z	protein	277	Gallus gallus	P14315 (AlphaFold model)
CD2-associated protein	0, 3, 6, 9, C, F, I, L, O, R, U, X	protein	29	homo sapiens	Q9Y5K6 (AlphaFold model)

Sequence of entity 1 (1, 4, 7, A, D, G, J, M, P, S, V, Y), FASTA

>3LK4_1 F-actin-capping protein subunit alpha-1 (chains 1, 4, 7, A, D, G, J, M, P, S, V, Y)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW
RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 2 (2, 5, 8, B, E, H, K, N, Q, T, W, Z), FASTA

>3LK4_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains 2, 5, 8, B, E, H, K, N, Q, T, W, Z)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN

Sequence of entity 3 (0, 3, 6, 9, C, F, I, L, O, R, U, X), FASTA

>3LK4_3 CD2-associated protein (chains 0, 3, 6, 9, C, F, I, L, O, R, U, X)
VNFDDIASSENLLHLTANRPKMPGRRLPG

Primary citation

Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Hernandez-Valladares, M., Kim, T., Kannan, B. et al. Nat Struct Mol Biol (2010) 17:497-503. DOI 10.1038/nsmb.1792 · PubMed

Other PDB entries of the same protein (UniProt P13127 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7DS6 1.69 Å, Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera…
3AA0 1.7 Å, Crystal structure of Actin Capping Protein in complex with the Cp-binding motif derived…
7DS4 1.85 Å, Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail…
3AA1 1.9 Å, Crystal structure of Actin capping protein in complex with the Cp-binding motif derived…
3AA6 1.9 Å, Crystal structure of Actin capping protein in complex with the Cp-binding motif derived…
3AA7 1.9 Å, Crystal structure of Actin capping protein
7DS2 1.95 Å, Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail
7DS8 1.95 Å, Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera…
9BLI 2.0 Å, Crystal structure of Actin capping protein in complex with a fragment of Legionella…
7DS3 2.09 Å, Crystal structure of actin capping protein in complex with twinflin-2 C-terminus tail
1IZN 2.1 Å, Crystal Structure of Actin Filament Capping Protein CapZ
3AAA 2.2 Å, Crystal Structure of Actin capping protein in complex with V-1

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