1ESV: Gelsolin

Complex between latrunculin a:rabbit muscle alpha actin:human gelsolin domain 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Jul 2000.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Homo sapiens, Oryctolagus cuniculus
Chains: 2
Atoms: 4,176
Mol. weight: 57.22 kDa
Ligands: CA, ATP, LAR
Released: 19 Jul 2000

Explore 1ESV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ESV contains 28 α-helices and 28 β-strands across 2 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: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	3
β-strand	16-21	6	3
β-strand	22	1	4
β-strand	24	1	4
β-strand	29-32	4	3
β-strand	35-38	4	5
β-strand	53-54	2	5
β-strand	65-68	4	5
β-strand	71-72	2	6
β-strand	75-76	2	6
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	3
α-helix	113-125	13
β-strand	131-136	6	3
α-helix	137-144	8
β-strand	150-155	6	7
β-strand	160-166	7	7
β-strand	169-170	2	7
α-helix	172-174	3
β-strand	176-178	3	7
α-helix	182-192	11
α-helix	194-196	3
α-helix	206-216	11
α-helix	223-230	8
β-strand	238-241	4	8
β-strand	247-250	4	8
α-helix	259-262	4
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	7
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	7
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	3
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain S: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
β-strand	16-23	8	1
β-strand	26-29	4	1
α-helix	30-31	2
α-helix	32-34	3
β-strand	37-39	3	2
β-strand	43-51	9	1
β-strand	57-65	9	1
α-helix	71-87	17
β-strand	92-98	7	1
α-helix	104-107	4
β-strand	115-117	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Gelsolin	S	protein	125	Homo sapiens	P06396 (AlphaFold model)
Alpha actin	A	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)

Sequence of entity 1 (S), FASTA

>1ESV_1 GELSOLIN (chains S)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTCLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGF

Sequence of entity 2 (A), FASTA

>1ESV_2 ALPHA ACTIN (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	3
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
LAR	Latrunculin a	C22 H31 N O5 S	1

Primary citation

Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Morton, W.M., Ayscough, K.R., McLaughlin, P.J. Nat Cell Biol (2000) 2:376-378. DOI 10.1038/35014075 · PubMed

Other PDB entries of the same protein (UniProt P06396 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5FAF 1.05 Å, N184K pathological variant of gelsolin domain 2 (orthorhombic form)
6QW3 1.3 Å, Calcium-bound gelsolin domain 2
6LJE 1.4 Å, Crystal structure of gelsolin G3 domain (calcium and magnesium condition)
6LJF 1.5 Å, Crystal structure of gelsolin G3 domain (calcium condition)
2FH1 1.55 Å, C-terminal half of gelsolin soaked in low calcium at pH 4.5
3CIP 1.6 Å, Complex of Dictyostelium Discoideum Actin with Gelsolin
1KCQ 1.65 Å, Human Gelsolin Domain 2 with a Cd2+ bound
3CI5 1.7 Å, Complex of Phosphorylated Dictyostelium Discoideum Actin with Gelsolin
5FAE 1.7 Å, N184K pathological variant of gelsolin domain 2 (trigonal form)
5O2Z 1.7 Å, Domain swap dimer of the G167R variant of gelsolin second domain
1D4X 1.75 Å, Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin…
1NLV 1.8 Å, Crystal Structure Of Dictyostelium Discoideum Actin Complexed With Ca ATP And Human…

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