Research workbench

HLA-dr antigens associated invariant chain

Analyse HLA-dr antigens associated invariant chain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IIE
Type: protein
Length: 225 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (HLA-dr antigens associated invariant chain)
UniProt: P04233
Pockets: 4 · best druggability 0.58

Structure

solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Protein (HLA-dr antigens associated invariant chain)	protein	75	56% helix, 0% strand	P04233

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.58	0.81	24	empty
2	84	0.37	0.77	21	empty
3	83	0.35	0.75	15	empty
4	81	0.33	0.75	22	empty

Interfaces

3 interfaces between chains.

B–C · 1441 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 1437 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1436 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1IIE · HLA-dr antigens associated invariant chain · the same entry in another collection · chain A against A, TM-score 1.00
P04233 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen gamma chain… · a predicted model of the same protein · chain A against A, TM-score 0.81

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04233
Elsewhere: RCSB PDB 1IIE · PDBe 1IIE · UniProt P04233

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