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UniProt Q13332

Q13332

Q13332 (UniProt Q13332): 13 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q13332
Experimental structures
13
Predicted models
0

Structures

13 records of Q13332 in the MolNFT archive: 13 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2FH7Crystal structure of the phosphatase domains of human PTP SIGMAx-ray diffractionA——
2FH7Crystal structure of the phosphatase domains of human ptp sigmax-ray diffractionA——
2YD2Crystal structure of the N-terminal Ig1-2 module of Human Receptor Protein Tyrosine Phosphatase…x-ray diffractionA——
2YD2Crystal structure of the N-terminal IG1-2 module of human receptor protein tyrosine phosphatase…x-ray diffractionA——
2YD3Crystal structure of the N-terminal Ig1-2 module of Human Receptor Protein Tyrosine Phosphatase…x-ray diffractionA——
2YD3Crystal structure of the N-terminal IG1-2 module of human receptor protein tyrosine phosphatase…x-ray diffractionA——
2YD9Crystal structure of the N-terminal Ig1-3 module of Human Receptor Protein Tyrosine Phosphatase…x-ray diffractionA——
2YD9Crystal structure of the N-terminal IG1-3 module of human receptor protein tyrosine phosphatase…x-ray diffractionA——
4BPCStructure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Formx-ray diffractionA——
4BPCStructure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid formx-ray diffractionA——
4PBXCrystal structure of the six N-terminal domains of human receptor protein tyrosine phosphatase sigmax-ray diffractionA——
4PBXCrystal structure of the six N-terminal domains of human receptor protein tyrosine phosphatase sigmax-ray diffractionA——
Q13332AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase S (Q13332)———

Elsewhere

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