5JP2: Epidermal growth factor receptor substrate 15

Fcho1 Mu homology domain (Danio Rerio) with bound Eps15 peptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 8 Jun 2016.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Homo sapiens, Danio rerio
Chains: 4
Atoms: 4,596
Mol. weight: 68.22 kDa
Ligands: ZN
Released: 8 Jun 2016

Explore 5JP2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JP2 contains 10 α-helices and 38 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: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	883-897	15	1
β-strand	905-918	14	1
α-helix	921-927	7
α-helix	931-934	4
β-strand	935-939	5	2
β-strand	946-949	4	1
β-strand	954-956	3	2
β-strand	965-970	6	2
α-helix	972-985	14
β-strand	991-1003	13	1
α-helix	1006-1008	3
β-strand	1011-1020	10	3
β-strand	1023-1032	10	3
β-strand	1042	1	4
β-strand	1043-1050	8	1
β-strand	1056-1061	6	3
β-strand	1065-1067	3	1
β-strand	1072-1076	5	1
β-strand	1080	1	4
α-helix	1085-1088	4
β-strand	1089-1097	9	3
β-strand	1108-1116	9	1
β-strand	1124-1127	4	2
β-strand	1132-1149	18	1

Chain B: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	883-897	15	5
β-strand	905-918	14	5
α-helix	921-927	7
α-helix	931-934	4
β-strand	935-939	5	6
β-strand	946-949	4	5
β-strand	954-956	3	6
β-strand	965-970	6	6
α-helix	972-985	14
β-strand	991-1003	13	5
α-helix	1006-1008	3
β-strand	1011-1020	10	7
β-strand	1023-1032	10	7
β-strand	1042	1	8
β-strand	1043-1050	8	5
β-strand	1056-1061	6	7
β-strand	1065-1067	3	5
β-strand	1072-1076	5	5
β-strand	1080	1	8
α-helix	1085-1088	4
β-strand	1089-1097	9	7
β-strand	1108-1116	9	5
β-strand	1124-1128	5	6
β-strand	1132-1149	18	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor substrate 15	E, F	protein	27	Homo sapiens	P42566 (AlphaFold model)
F-BAR domain only protein 1	A, B	protein	286	Danio rerio	A0A0R4IA99

Sequence of entity 1 (E, F), FASTA

>5JP2_1 Epidermal growth factor receptor substrate 15 (chains E, F)
TNLDFFQSDPFVGSDPFKDDPFGGAGA

Sequence of entity 2 (A, B), FASTA

>5JP2_2 F-BAR domain only protein 1 (chains A, B)
GLSRGPSPISLSAQESWPVAAAITEYINAYFRGGEHNRCLVKITGDLTMSFPAGITRIFT
ANPNAPVLSFRLVNISRVDHFLPNQKLLYSDPSQSDPDTKDFWFNMQALTLHLQREAELN
PQASYYNVALLKYQASSQDPSRAPLLLSAECQRSGTVTRVSLDYHCCPATAPATQLTSVQ
VLLPLDHSATDLQCQPPAAWNAEERRLLWKLANLSPTNHSKGSGTLCASWQCLEVPRGPA
PSLAVQFVGSGASLSGLDVELVGSRYRMSLVKKRFATGKYMAGCSL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Transient Fcho1/2Eps15/RAP-2 Nanoclusters Prime the AP-2 Clathrin Adaptor for Cargo Binding. Ma, L., Umasankar, P.K., Wrobel, A.G. et al. Dev Cell (2016) 37:428-443. DOI 10.1016/j.devcel.2016.05.003 · PubMed

Other PDB entries of the same protein (UniProt P42566 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4RHG 1.58 Å, Crystal structure of PTPN3 (PTPH1) D811E, C842S mutant in complex with Eps15 pTyr849…
4RH9 1.6 Å, Crystal structure of PTPN3 (PTPH1) H812F, M883G mutant in complex with Eps15 pTyr849…
4RH5 1.6 Å, Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 peptide
4S0G 1.72 Å, Crystal structure of PTPN3 (PTPH1) in complex with Eps15 pTyr849 P850V peptide
2IV9 1.9 Å, B2-appendage from AP2 in complex with Eps15 peptide
5AWU 2.7 Å, Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment…
5AWT 2.7 Å, Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment…
1C07 Structure of the third EPS15 homology domain of human EPS15
1EH2 Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures
1F8H Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfr
1FF1 Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfl
2JXC Structure of the EPS15-EH2 Stonin2 Complex

Browse structure collections

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