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Crystal structure of truncated human beta-B1-crystallin

Analyse Crystal structure of truncated human beta-B1-crystallin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OKI
Type: protein
Length: 366 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta crystallin B1
UniProt: P53674
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta crystallin B1	protein	183	10% helix, 48% strand	P53674

Pockets

2 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	309	0.70	0.84	61	empty
2	59	0.28	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1673 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

1OKI · Crystal structure of truncated human beta-B1-crystallin · the same entry in another collection · chain A against A, TM-score 1.00
P53674 · AlphaFold monomer V2.0 prediction for beta-crystallin B1 (P53674) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P53674
Elsewhere: RCSB PDB 1OKI · PDBe 1OKI · UniProt P53674

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