Helical reconstruction of ACAP1(BAR-PH domain) decorated membrane tubules by cryo-electron microscopy. Determined by electron microscopy at 17.0 Å resolution. Released 15 Oct 2014.
Explore 4CKH in 3D Show helices and sheets RCSB PDB PDBe
4CKH contains 48 α-helices and 44 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 15-68 | 54 | |
| α-helix | 74-105 | 32 | |
| α-helix | 106-110 | 5 | |
| α-helix | 111-116 | 6 | |
| α-helix | 118-143 | 26 | |
| β-strand | 145 | 1 | 1 |
| α-helix | 149-208 | 60 | |
| α-helix | 210-248 | 39 | |
| α-helix | 254-257 | 4 | |
| β-strand | 260 | 1 | 2 |
| α-helix | 262-265 | 4 | |
| β-strand | 267 | 1 | 2 |
| β-strand | 268-275 | 8 | 3 |
| β-strand | 284-291 | 8 | 3 |
| β-strand | 294-298 | 5 | 3 |
| α-helix | 304-305 | 2 | |
| β-strand | 306-307 | 2 | 3 |
| β-strand | 316-319 | 4 | 3 |
| β-strand | 325 | 1 | 4 |
| β-strand | 328-332 | 5 | 3 |
| β-strand | 338-341 | 4 | 3 |
| α-helix | 345-363 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-2 | 2 | |
| α-helix | 7-12 | 6 | |
| α-helix | 15-69 | 55 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-105 | 25 | |
| α-helix | 106-110 | 5 | |
| α-helix | 111-115 | 5 | |
| α-helix | 118-142 | 25 | |
| β-strand | 145 | 1 | 4 |
| α-helix | 150-244 | 95 | |
| α-helix | 245-249 | 5 | |
| β-strand | 260-261 | 2 | 5 |
| β-strand | 266-267 | 2 | 5 |
| β-strand | 268-275 | 8 | 6 |
| β-strand | 283-291 | 9 | 6 |
| β-strand | 294-298 | 5 | 6 |
| β-strand | 306-309 | 4 | 6 |
| β-strand | 316-318 | 3 | 6 |
| β-strand | 325 | 1 | 1 |
| β-strand | 328-332 | 5 | 6 |
| β-strand | 337-341 | 5 | 6 |
| α-helix | 345-359 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arf-gap with coiled-coil, ank repeat and PH domain-containing protein 1 | A, B, C, D | protein | 382 | HOMO SAPIENS | Q15027 (AlphaFold model) |
>4CKH_1 ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1 (chains A, B, C, D) GPLGSMTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAA SRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKE GLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYAL QINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREK RDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQL VYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAV QSSIASAFSQARLDDSPRGPGQ
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. 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:
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