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UniProt P31483

Nucleolysin TIA-1 isoform p40 (P31483)

Nucleolysin TIA-1 isoform p40 (UniProt P31483): 15 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P31483
Protein
Nucleolysin TIA-1 isoform p40
Experimental structures
15
Predicted models
0

Structures

15 records of P31483 in the MolNFT archive: 15 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2MJNStructure, dynamics and RNA binding of the multi-domain splicing factor TIA-1solution nmrA——
2MJNStructure, dynamics and RNA binding of the multi-domain splicing factor tia-1solution nmrA——
3BS9X-ray structure of human TIA-1 RRM2x-ray diffractionA, B——
3BS9X-ray structure of human tia-1 RRM2x-ray diffractionA, B——
5ITHTIA-1 RRM2 recognition of target oligonucleotidex-ray diffractionA——
5ITHTia-1 RRM2 recognition of target oligonucleotidex-ray diffractionA——
5O2VNMR structure of TIA-1 RRM1 domainsolution nmrA——
5O2VNMR structure of tia-1 RRM1 domainsolution nmrA——
5O3JCrystal structure of TIA-1 RRM2 in complex with RNAx-ray diffractionA——
5O3JCrystal structure of tia-1 RRM2 in complex with RNAx-ray diffractionA——
6ELDCrystal structure of TIA-1 RRM1 in complex with U1Cx-ray diffractionA——
6ELDCrystal structure of tia-1 RRM1 in complex with U1Cx-ray diffractionA——
7VI4Electron crystallographic structure of TIA-1 prion-like domain, A381T mutantelectron crystallographyA——
7VI5Electron crystallographic structure of TIA-1 prion-like domain, wild type sequenceelectron crystallographyA——
P31483AlphaFold monomer V2.0 prediction for nucleolysin tia-1 isoform P40 (P31483)———

Elsewhere

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