9NGE: PDB entry 9NGE

The ubiquitin-associated domain of human thirty-eight negative kinase-1 rigidly fused to a double trigger variant of the 1TEL crystallization chaperone. Determined by X-ray diffraction at 2.02 Å resolution. Released 26 Mar 2025.

Method
X-ray diffraction
Resolution
2.02 Å
Organism
Homo sapiens
Chains
2
Atoms
2,424
Mol. weight
39.11 kDa
Released
26 Mar 2025

Explore 9NGE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9NGE contains 22 α-helices and 0 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: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix18-203
α-helix24-263
α-helix29-4214
α-helix45-473
α-helix57-604
α-helix65-717
α-helix76-10025
α-helix106-1149
α-helix120-13617
α-helix140-14910
α-helix154-1629
Chain B: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix18-203
α-helix24-263
α-helix29-4214
α-helix45-473
α-helix57-604
α-helix65-717
α-helix76-10025
α-helix106-11611
α-helix120-13516
α-helix140-14910
α-helix154-16310

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1A, Bprotein165Homo sapiensP41212 (AlphaFold model), Q13470 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9NGE_1 Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1 (chains A, B)
MGHHHHHHHHHHSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLSPIDSNTFEMNGKAL
LELTKEDFRYRSPHSGDELYELLQHILKEVQRKIMEVELSVHGVTHQEAQTALGATGGDV
VSAIRNLKVDQLFHLSSRSRADAWRILEHYQWDLSAASRYVLARP

Primary citation

The ubiquitin-associated domain of human thirty-eight negative kinase-1 rigidly fused to a double trigger variant of the 1TEL crystallization chaperone. Averett, J.C. To be published.

Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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