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Crystal structure of the pH-beach domains of human LRBA/BGL

Analyse Crystal structure of the pH-beach domains of human LRBA/BGL in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T77
Type: protein
Length: 1,656 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipopolysaccharide-responsive and beige-like anchor protein
UniProt: P50851
Pockets: 12 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Lipopolysaccharide-responsive and beige-like anchor protein	protein	414	38% helix, 14% strand	P50851

Pockets

12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	691	0.70	0.78	72	empty
2	672	0.69	0.77	74	empty
3	514	0.67	0.78	56	empty
4	430	0.60	0.75	50	empty
5	426	0.59	0.75	49	empty

Interfaces

2 interfaces between chains.

A–B · 230 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 163 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1T77 · Crystal structure of the PH-BEACH domains of human LRBA/BGL · the same entry in another collection · chain A against A, TM-score 1.00

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 P50851
Elsewhere: RCSB PDB 1T77 · PDBe 1T77 · UniProt P50851

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