6FNG: Ephrin type-A receptor 2

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with an isomer of NVP-BHG712. Determined by X-ray diffraction at 1.04 Å resolution. Released 8 Aug 2018.

Method
X-ray diffraction
Resolution
1.04 Å
Organism
Homo sapiens
Chains
1
Atoms
2,615
Mol. weight
35.34 kDa
Ligands
DWT
Released
8 Aug 2018

Explore 6FNG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6FNG contains 19 α-helices and 12 β-strands across 1 chain. 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: 19 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix600-6023
β-strand60711
α-helix610-6123
β-strand613-62191
β-strand626-63271
β-strand641-64881
α-helix654-66916
β-strand67512
α-helix676-6772
β-strand678-68251
β-strand688-69361
β-strand69912
α-helix700-7067
α-helix713-73220
α-helix742-7443
β-strand745-74732
β-strand753-75532
α-helix781-7833
α-helix786-7916
α-helix796-81116
α-helix815-8162
α-helix823-8319
α-helix836-8394
β-strand84313
α-helix844-85310
α-helix858-8603
α-helix862-8632
α-helix864-87613
α-helix878-8814
β-strand88413
α-helix885-8873

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ephrin type-A receptor 2Aprotein306Homo sapiensP29317 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6FNG_1 Ephrin type-A receptor 2 (chains A)
GDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTE
KQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVL
QLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTT
SGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGF
RLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIR
LPSTSG

Ligands and cofactors

IDNameFormulaCopies
DWT4-methyl-3-[(2-methyl-6-pyridin-3-yl-pyrazolo[3,4-d]pyrimidin-4-yl)amino]-~{N}-…C26 H20 F3 N7 O1

Water and common crystallization additives (EDO) are not listed.

Primary citation

NVP-BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family. Troster, A., Heinzlmeir, S., Berger, B.T. et al. ChemMedChem (2018) 13:1629-1633. DOI 10.1002/cmdc.201800398 · PubMed

Other PDB entries of the same protein (UniProt P29317 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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