7W52: Fragmin domain-1

Crystal structure of fragmin domain-1 (15-160) in complex with actin. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Oct 2022.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Gallus gallus, Physarum polycephalum
Chains: 8
Atoms: 17,256
Mol. weight: 237.88 kDa
Ligands: ATP, CA
Released: 26 Oct 2022

Explore 7W52 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7W52 contains 135 α-helices and 112 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.

Chain A: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-37	3	3
β-strand	53-54	2	3
α-helix	56-60	5
α-helix	62-64	3
β-strand	66-68	3	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	5
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-353	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chains B and F: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	20-30	11
α-helix	34-36	3
β-strand	44-51	8	7
β-strand	54-57	4	7
α-helix	58-59	2
α-helix	60-62	3
β-strand	65-67	3	8
β-strand	71-78	8	7
β-strand	88-95	8	7
α-helix	101-117	17
β-strand	123-128	6	7
α-helix	134-137	4
β-strand	146-148	3	8
α-helix	152-154	3
α-helix	156	1
β-strand	157	1	2
α-helix	158	1

Chain C: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	9
β-strand	16-21	6	9
β-strand	24	1	10
β-strand	29-32	4	9
β-strand	35-36	2	11
β-strand	53-54	2	11
α-helix	55-58	4
β-strand	67-68	2	11
β-strand	71-72	2	12
β-strand	75-76	2	12
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	9
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	9
α-helix	137-144	8
β-strand	150-155	6	13
β-strand	160-166	7	13
β-strand	169-170	2	13
α-helix	172-174	3
β-strand	176-178	3	13
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	14
α-helix	246	1
β-strand	247-250	4	14
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	13
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	13
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	9
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	21-30	10
α-helix	34-36	3
β-strand	44-51	8	15
β-strand	54-57	4	15
α-helix	58-59	2
α-helix	60-62	3
β-strand	65-67	3	16
β-strand	71-78	8	15
β-strand	88-95	8	15
α-helix	101-117	17
β-strand	123-128	6	15
α-helix	134-137	4
β-strand	146-148	3	16
α-helix	152-154	3
α-helix	156	1
β-strand	157	1	10
α-helix	158-159	2

Chain E: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	17
β-strand	16-21	6	17
β-strand	24	1	18
β-strand	29-32	4	17
β-strand	35-36	2	19
β-strand	53-54	2	19
α-helix	56-59	4
β-strand	67-68	2	19
β-strand	71-72	2	20
β-strand	75-76	2	20
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	17
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	17
α-helix	137-144	8
β-strand	150-155	6	21
β-strand	160-166	7	21
β-strand	169-170	2	21
α-helix	172-174	3
β-strand	176-178	3	21
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	21
α-helix	302-304	3
α-helix	309-318	10
β-strand	329-330	2	21
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	17
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain G: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	25
β-strand	16-21	6	25
β-strand	24	1	26
β-strand	29-32	4	25
β-strand	35	1	27
β-strand	54	1	27
β-strand	68	1	27
β-strand	71-72	2	28
β-strand	75-76	2	28
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	25
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	25
α-helix	137-144	8
β-strand	150-155	6	29
β-strand	160-166	7	29
β-strand	169-170	2	29
α-helix	172-174	3
β-strand	176-178	3	29
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	30
β-strand	247-250	4	30
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	29
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	29
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-353	4
β-strand	357-358	2	25
α-helix	359-365	7
α-helix	367-372	6

Chain H: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	20-30	11
α-helix	34-36	3
β-strand	44-51	8	31
β-strand	54-57	4	31
α-helix	58-59	2
α-helix	60-62	3
β-strand	65-67	3	32
β-strand	71-78	8	31
β-strand	88-95	8	31
α-helix	101-117	17
β-strand	123-128	6	31
α-helix	134-137	4
β-strand	146-148	3	32
α-helix	152-154	3
α-helix	156	1
β-strand	157	1	26
α-helix	158-159	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, C, E, G	protein	377	Gallus gallus	P68139 (AlphaFold model)
Actin-binding protein fragmin P	B, D, F, H	protein	148	Physarum polycephalum	Q94707 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>7W52_1 Actin, alpha skeletal muscle (chains A, C, E, G)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (B, D, F, H), FASTA

>7W52_2 Actin-binding protein fragmin P (chains B, D, F, H)
GPANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPVPKKHHGSFYTGDSY
IVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYLGGLPVQYREVQGYE
SERFLSLFPKGGLRILDGGVETGFHHVE

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	4
CA	Calcium ion	Ca	12

Water and common crystallization additives (ACT, NA, EDO) are not listed.

Primary citation

Structures and mechanisms of actin ATP hydrolysis. Kanematsu, Y., Narita, A., Oda, T. et al. Proc Natl Acad Sci U S A (2022) 119:e2122641119-e2122641119. DOI 10.1073/pnas.2122641119 · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W4Z 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
7W50 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-Pi-form)
7W51 1.2 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-form)
9L2N 1.7 Å, Crystal structure of Cytochalasin D bound to a filamentous conformation actin
1MDU 2.2 Å, Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1…
8D13 2.43 Å, Helical ADP-F-actin
8D14 2.51 Å, Helical ADP-Pi-F-actin
7R94 2.6 Å, T-Plastin-F-actin complex
8C4E 2.6 Å, F-actin decorated by SipA426-685
9JW0 2.69 Å, Structure of the N-terminal 3 domains (V1-V3) villin bound to actin
7YNE 2.7 Å, Crystal structure of fragmin domain-1 (1-160) in complex with G-form actin
8C4C 2.7 Å, F-actin decorated by SipA497-669

Browse structure collections

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