4B1Z: Phactr1 RPEL domain

Structure of the Phactr1 RPEL domain bound to G-actin. Determined by X-ray diffraction at 3.3 Å resolution. Released 7 Nov 2012.

Method: X-ray diffraction
Resolution: 3.3 Å
Organisms: ORYCTOLAGUS CUNICULUS, MUS MUSCULUS
Chains: 8
Atoms: 17,941
Mol. weight: 283.76 kDa
Ligands: MG, ATP
Released: 7 Nov 2012

Explore 4B1Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4B1Z contains 154 α-helices and 111 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: 22 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	71-72	2	2
β-strand	75-76	2	2
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	3
β-strand	160-166	7	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	176-178	3	3
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	4
β-strand	247-250	4	4
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	3
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	333-337	5
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	5
β-strand	16-21	6	5
β-strand	29-32	4	5
β-strand	35-37	3	6
β-strand	53-54	2	6
α-helix	56-60	5
β-strand	66-68	3	6
β-strand	71-72	2	7
β-strand	75-76	2	7
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	5
α-helix	113-125	13
β-strand	131-136	6	5
α-helix	137-144	8
β-strand	150-155	6	8
β-strand	160-166	7	8
β-strand	169-170	2	8
α-helix	172-174	3
β-strand	176-178	3	8
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	9
β-strand	247-250	4	9
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	8
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	8
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	5
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain C: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	10
β-strand	16-21	6	10
β-strand	29-32	4	10
β-strand	35-38	4	11
β-strand	53-54	2	11
α-helix	56-60	5
β-strand	65-68	4	11
β-strand	71-72	2	12
β-strand	75-76	2	12
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	10
α-helix	113-127	15
β-strand	131-136	6	10
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	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	14
β-strand	247-250	4	14
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	287-294	8
β-strand	297-300	4	13
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	13
α-helix	333-337	5
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	10
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain D: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	15
β-strand	16-21	6	15
β-strand	29-32	4	15
β-strand	35-36	2	16
β-strand	53-54	2	16
α-helix	56-60	5
β-strand	67-68	2	16
β-strand	71-72	2	17
β-strand	75-76	2	17
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	15
α-helix	113-125	13
β-strand	131-136	6	15
α-helix	137-144	8
β-strand	150-155	6	18
β-strand	160-166	7	18
β-strand	169-170	2	18
α-helix	172-174	3
β-strand	176-178	3	18
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	19
β-strand	247-250	4	19
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	18
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	18
α-helix	333-337	5
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	15
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain E: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	20
β-strand	16-21	6	20
β-strand	29-32	4	20
β-strand	35-38	4	21
β-strand	53-54	2	21
α-helix	56-60	5
β-strand	65-68	4	21
β-strand	71-72	2	22
β-strand	75-76	2	22
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	20
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	20
α-helix	137-144	8
β-strand	150-155	6	23
β-strand	160-166	7	23
β-strand	169-170	2	23
α-helix	172-174	3
β-strand	176-178	3	23
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	24
β-strand	247-250	4	24
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	287-294	8
β-strand	297-300	4	23
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	23
α-helix	333-337	5
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	20
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain F: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	25
β-strand	16-21	6	25
β-strand	29-32	4	25
β-strand	35-37	3	26
β-strand	53-54	2	26
α-helix	56-60	5
β-strand	66-68	3	26
β-strand	71-72	2	27
β-strand	75-76	2	27
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	25
α-helix	113-125	13
β-strand	131-136	6	25
α-helix	137-144	8
β-strand	150-155	6	28
β-strand	160-166	7	28
β-strand	169-170	2	28
α-helix	172-174	3
β-strand	176-178	3	28
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	29
β-strand	247-250	4	29
α-helix	253-259	7
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	28
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	28
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	25
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain M: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	420-428	9
α-helix	431-433	3
α-helix	434-439	6
α-helix	448-468	21
α-helix	472-476	5
α-helix	486-505	20
α-helix	510-515	6

Chain N: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	423-429	7
α-helix	431-433	3
α-helix	434-439	6
α-helix	448-467	20
α-helix	469-471	3
α-helix	472-476	5
α-helix	486-505	20
α-helix	510-515	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F	protein	376	ORYCTOLAGUS CUNICULUS	P68135 (AlphaFold model)
Phosphatase and actin regulator 1	M, N	protein	115	MUS MUSCULUS	Q2M3X8 (AlphaFold model)

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

>4B1Z_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B, C, D, E, F)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF

Sequence of entity 2 (M, N), FASTA

>4B1Z_2 PHOSPHATASE AND ACTIN REGULATOR 1 (chains M, N)
LAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAE
ELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEV

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	6
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	6

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

Primary citation

Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity. Mouilleron, S., Wiezlak, M., O'Reilly, N. et al. Structure (2012) 20:1960-1970. DOI 10.1016/j.str.2012.08.031 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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