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Crystal structure of human ig-beta homodimer

Analyse Crystal structure of human ig-beta homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KG5
Type: protein
Length: 206 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: B-cell antigen receptor complex-associated protein beta chain
UniProt: P40259
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	B-cell antigen receptor complex-associated protein beta chain	protein	103	0% helix, 48% strand	P40259

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	439	0.69	0.80	47	empty

Interfaces

1 interface between chains.

A–B · 522 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3KG5 · Crystal structure of human Ig-beta homodimer · the same entry in another collection · chain A against A, TM-score 1.00
P40259 · AlphaFold monomer V2.0 prediction for B-cell antigen receptor complex-associated protein… · a predicted model of the same protein · chain B against A, TM-score 0.91

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 P40259
Elsewhere: RCSB PDB 3KG5 · PDBe 3KG5 · UniProt P40259

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