4NSW: BAR-PH domain of ACAP1

Crystal structure of the BAR-PH domain of ACAP1. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Oct 2014.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,985
Mol. weight: 86.67 kDa
Released: 15 Oct 2014

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

Secondary structure: helices and β-sheets

4NSW contains 29 α-helices and 21 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	7-12	6
α-helix	15-68	54
α-helix	74-104	31
α-helix	105-110	6
α-helix	111-113	3
α-helix	115-117	3
α-helix	118-143	26
β-strand	145	1	1
α-helix	149-212	64
α-helix	214-248	35
α-helix	253-257	5
β-strand	258-260	3	2
β-strand	267-275	9	2
β-strand	283-291	9	2
β-strand	294-298	5	2
α-helix	304-305	2
β-strand	306-309	4	2
α-helix	312-314	3
β-strand	315-319	5	2
β-strand	325	1	3
β-strand	328-333	6	2
β-strand	337-341	5	2
α-helix	345-361	17

Chain B: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	1-3	3
α-helix	7-12	6
α-helix	15-67	53
α-helix	74-104	31
α-helix	105-110	6
α-helix	111-113	3
α-helix	115-117	3
α-helix	118-143	26
β-strand	145	1	3
α-helix	151-212	62
α-helix	214-244	31
α-helix	245-249	5
α-helix	253-255	3
α-helix	257-259	3
β-strand	260-262	3	4
β-strand	265-267	3	4
β-strand	268-275	8	5
β-strand	283-291	9	5
β-strand	294-298	5	5
α-helix	303-305	3
β-strand	306-309	4	5
α-helix	312-314	3
β-strand	316-319	4	5
β-strand	325	1	1
β-strand	328-332	5	5
β-strand	337-341	5	5
α-helix	345-358	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1	A, B	protein	382	Homo sapiens	Q15027 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4NSW_1 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (chains A, B)
GPLGSMTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAA
SRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKE
GLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYAL
QINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREK
RDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQL
VYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAV
QSSIASAFSQARLDDSPRGPGQ

Primary citation

A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature. Pang, X., Fan, J., Zhang, Y. et al. Dev Cell (2014) 31:73-86. DOI 10.1016/j.devcel.2014.08.020 · PubMed

Other PDB entries of the same protein (UniProt Q15027 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3JUE 2.3 Å, Crystal Structure of ArfGAP and ANK repeat domain of ACAP1
3T9K 2.3 Å, Crystal Structure of ACAP1 C-portion mutant S554D fused with integrin beta1 peptide
4F1P 2.3 Å, Crystal Structure of mutant S554D for ArfGAP and ANK repeat domain of ACAP1
5H3D 14.0 Å, Helical structure of membrane tubules decorated by ACAP1 (BARPH doamin) protein by…
4CKG 15.0 Å, Helical reconstruction of ACAP1(BAR-PH domain) decorated membrane tubules by…
4CKH 17.0 Å, Helical reconstruction of ACAP1(BAR-PH domain) decorated membrane tubules by…

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