4EDL: Beta-parvin CH2 domain
Crystal structure of beta-parvin CH2 domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Aug 2012.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 6,593
- Mol. weight
- 93.28 kDa
- Released
- 8 Aug 2012
Explore 4EDL in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4EDL contains 57 α-helices and 0 β-strands across 6 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: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 241-246 | 6 | |
| α-helix | 250-268 | 19 | |
| α-helix | 269-271 | 3 | |
| α-helix | 286-295 | 10 | |
| α-helix | 312-328 | 17 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-360 | 15 | |
Chain B: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 241-248 | 8 | |
| α-helix | 250-253 | 4 | |
| α-helix | 254-268 | 15 | |
| α-helix | 269-271 | 3 | |
| α-helix | 278-281 | 4 | |
| α-helix | 286-295 | 10 | |
| α-helix | 302-304 | 3 | |
| α-helix | 312-328 | 17 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-360 | 15 | |
Chain C: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 241-248 | 8 | |
| α-helix | 250-268 | 19 | |
| α-helix | 269-271 | 3 | |
| α-helix | 286-295 | 10 | |
| α-helix | 299-301 | 3 | |
| α-helix | 302-304 | 3 | |
| α-helix | 312-328 | 17 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-360 | 15 | |
Chain D: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 243-246 | 4 | |
| α-helix | 253-268 | 16 | |
| α-helix | 269-271 | 3 | |
| α-helix | 278-281 | 4 | |
| α-helix | 286-295 | 10 | |
| α-helix | 302-304 | 3 | |
| α-helix | 312-328 | 17 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-360 | 15 | |
Chain E: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 241-248 | 8 | |
| α-helix | 250-268 | 19 | |
| α-helix | 269-271 | 3 | |
| α-helix | 286-295 | 10 | |
| α-helix | 302-304 | 3 | |
| α-helix | 312-328 | 17 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-359 | 14 | |
Chain F: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 241-248 | 8 | |
| α-helix | 250-268 | 19 | |
| α-helix | 269-271 | 3 | |
| α-helix | 286-295 | 10 | |
| α-helix | 302-304 | 3 | |
| α-helix | 312-329 | 18 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 346-360 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Beta-parvin | A, B, C, D, E, F | protein | 133 | Homo sapiens | Q9HBI1 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>4EDL_1 Beta-parvin (chains A, B, C, D, E, F)
GNSGRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLL
MGLLEDYFVPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLR
VLYNLFTKYKNVE
Primary citation
Structural basis for paxillin binding and focal adhesion targeting of beta-parvin. Stiegler, A.L., Draheim, K.M., Li, X. et al. J Biol Chem (2012) 287:32566-32577. DOI 10.1074/jbc.M112.367342 · PubMed
Other PDB entries of the same protein (UniProt Q9HBI1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4EDM 2.0 Å, Crystal structure of beta-parvin CH2 domain
- 4EDN 2.9 Å, Crystal structure of beta-parvin CH2 domain in complex with paxillin LD1 motif
Browse structure collections
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