4EDN: Beta-parvin CH2 domain

Crystal structure of beta-parvin CH2 domain in complex with paxillin LD1 motif. Determined by X-ray diffraction at 2.9 Å resolution. Released 8 Aug 2012.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 17
Atoms: 11,011
Mol. weight: 169.22 kDa
Released: 8 Aug 2012

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

Secondary structure: helices and β-sheets

4EDN contains 112 α-helices and 0 β-strands across 17 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	241-248	8
α-helix	250-252	3
α-helix	253-268	16
α-helix	269-271	3
α-helix	278-281	4
α-helix	286-295	10
α-helix	299-301	3
α-helix	312-328	17
α-helix	331-334	4
α-helix	338-342	5
α-helix	346-359	14

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	241-247	7
α-helix	250-268	19
α-helix	269-271	3
α-helix	286-296	11
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	346-359	14

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	241-247	7
α-helix	250-252	3
α-helix	253-268	16
α-helix	269-271	3
α-helix	278-281	4
α-helix	286-295	10
α-helix	299-301	3
α-helix	312-329	18
α-helix	331-334	4
α-helix	338-342	5
α-helix	346-360	15

Chain D: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	243-247	5
α-helix	253-268	16
α-helix	269-271	3
α-helix	286-295	10
α-helix	299-301	3
α-helix	312-329	18
α-helix	331-334	4
α-helix	338-342	5
α-helix	346-359	14

Chain E: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	241-247	7
α-helix	250-252	3
α-helix	253-268	16
α-helix	269-271	3
α-helix	278-281	4
α-helix	286-295	10
α-helix	299-301	3
α-helix	302-304	3
α-helix	312-328	17
α-helix	332-334	3
α-helix	338-342	5
α-helix	346-359	14

Chain F: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	241-245	5
α-helix	250-252	3
α-helix	253-268	16
α-helix	269-271	3
α-helix	286-295	10
α-helix	299-301	3
α-helix	312-328	17
α-helix	331-334	4
α-helix	338-342	5
α-helix	346-359	14

Chain G: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	242-247	6
α-helix	250-252	3
α-helix	253-268	16
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	346-359	14

Chain H: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	241-247	7
α-helix	253-268	16
α-helix	269-271	3
α-helix	278-281	4
α-helix	286-295	10
α-helix	299-301	3
α-helix	312-329	18
α-helix	332-334	3
α-helix	338-342	5
α-helix	346-359	14

7 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-parvin	A, B, C, D, E, F, G, H, I, J	protein	133	Homo sapiens	Q9HBI1 (AlphaFold model)
Paxillin	K, L, M, N, O, P, Q	protein	22	Homo sapiens	P49023 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA

>4EDN_1 Beta-parvin (chains A, B, C, D, E, F, G, H, I, J)
GNSGRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLL
MGLLEDYFVPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLR
VLYNLFTKYKNVE

Sequence of entity 2 (K, L, M, N, O, P, Q), FASTA

>4EDN_2 Paxillin (chains K, L, M, N, O, P, Q)
XMDDLDALLADLESTTSHISKX

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
4EDL 2.1 Å, Crystal structure of beta-parvin CH2 domain

Browse structure collections

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