2HLE: Ephrin type-B receptor 4

Structural and biophysical characterization of the EPHB4-EPHRINB2 protein protein interaction and receptor specificity. Determined by X-ray diffraction at 2.05 Å resolution. Released 22 Aug 2006.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,564
Mol. weight: 37.14 kDa
Released: 22 Aug 2006

Explore 2HLE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HLE contains 3 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: 1 helix, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17-22	6	1
β-strand	33-35	3	2
β-strand	43-48	6	1
β-strand	54-61	8	1
β-strand	71-74	4	2
β-strand	78-79	2	2
β-strand	86-94	9	1
β-strand	95	1	3
α-helix	97-99	3
β-strand	108	1	4
β-strand	110-118	9	2
β-strand	132	1	5
β-strand	135	1	5
β-strand	136-142	7	2
β-strand	147	1	3
β-strand	148-150	3	6
β-strand	154-156	3	6
β-strand	160-166	7	1
β-strand	173-180	8	2
β-strand	183	1	4
β-strand	184-195	12	1

Chain B: 2 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	7
β-strand	36-37	2	7
β-strand	46	1	8
β-strand	50	1	8
β-strand	51-53	3	9
α-helix	55-56	2
β-strand	60-65	6	7
β-strand	78	1	10
β-strand	79-81	3	11
β-strand	82-83	2	9
α-helix	86-89	4
β-strand	93	1	12
β-strand	102-104	3	11
β-strand	111-116	6	7
β-strand	133-134	2	13
β-strand	137-138	2	9
β-strand	143	1	10
β-strand	152	1	12
β-strand	162-165	4	9
β-strand	166-167	2	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ephrin type-B receptor 4	A	protein	188	Homo sapiens	P54760 (AlphaFold model)
Ephrin-B2	B	protein	138	Homo sapiens	P52799 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2HLE_1 Ephrin type-B receptor 4 (chains A)
AGHHHHHHEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPG
QAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTP
AWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALL
SLHLFYKK

Sequence of entity 2 (B), FASTA

>2HLE_2 Ephrin-B2 (chains B)
IVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQAD
RCTIKKENTPLLNCARPDQDVKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDN
QEGGVCQTRAMKILMKVG

Primary citation

Structural and Biophysical Characterization of the EphB4-EphrinB2 Protein-Protein Interaction and Receptor Specificity. Chrencik, J.E., Brooun, A., Kraus, M.L. et al. J Biol Chem (2006) 281:28185-28192. DOI 10.1074/jbc.M605766200 · PubMed

Other PDB entries of the same protein (UniProt P54760 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6FNK 1.05 Å, Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase with a…
6FNM 1.16 Å, Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase with Dasatinib
6FNJ 1.24 Å, Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase with an isomer of…
6FNL 1.27 Å, Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase
6FNI 1.47 Å, Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase with NVP-BHG712
2BBA 1.65 Å, Crystal Structure and Thermodynamic Characterization of the EphB4 Receptor in Complex…
2VWX 1.65 Å, ephB4 kinase domain inhibitor complex
2VWY 1.65 Å, ephB4 kinase domain inhibitor complex
2VWZ 1.65 Å, ephB4 kinase domain inhibitor complex
2VX1 1.65 Å, ephB4 kinase domain inhibitor complex
4BB4 1.65 Å, ephB4 kinase domain inhibitor complex
2XVD 1.7 Å, ephB4 kinase domain inhibitor complex

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