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UniProt P17693

HLA class I histocompatibility antigen, alpha chain G (P17693)

HLA class I histocompatibility antigen, alpha chain G (UniProt P17693): 16 experimental structures on GenesisL1, 1 ligand bound, 10 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P17693
Protein
HLA class I histocompatibility antigen, alpha chain G
Experimental structures
16
Predicted models
0
Ligands
1
Pockets
10 · 1 record with a druggable one

Structures

16 records of P17693 in the MolNFT archive: 16 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1YDP1.9A crystal structure of HLA-Gx-ray diffractionA——
1YDP1.9A crystal structure of HLA-Gx-ray diffractionA——
2D31Crystal structure of disulfide-linked HLA-G dimerx-ray diffractionA, D——
2D31Crystal structure of disulfide-linked HLA-G dimerx-ray diffractionA, D——
2DYPCrystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-Gx-ray diffractionA——
2DYPCrystal structure of LILRB2(LIR2/ILT4/CD85D) complexed with HLA-Gx-ray diffractionA——
3BZEThe human non-classical major histocompatibility complex molecule HLA-Ex-ray diffractionP, Q, R, S——
3BZEThe human non-classical major histocompatibility complex molecule HLA- Ex-ray diffractionP, Q, R, S——
3CDGHuman CD94/NKG2A in complex with HLA-Ex-ray diffractionP, Q——
3CDGHuman CD94/NKG2A in complex with HLA-Ex-ray diffractionP, Q——
3CIIStructure of NKG2A/CD94 bound to HLA-Ex-ray diffractionC, F——
3CIIStructure of NKG2A/CD94 bound to HLA-Ex-ray diffractionC, F——
6AEECrystal structure of the four ig-like domains of LILRB1 complexed with HLA-Gx-ray diffractionA, D——
6K60Structural and functional basis for HLA-G isoform recognition of immune checkpoint receptor LILRBsx-ray diffractionA, EIOD10 (best 0.79)
6K60Structural and functional basis for HLA-G isoform recognition of immune checkpoint receptor lilrbsx-ray diffractionA, EIOD—
P17693AlphaFold monomer V2.0 prediction for HLA class I histocompatibility antigen, alpha chain G (P17693)———

Ligands

  • IOD · Iodide ion · in 2 records

Elsewhere

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