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Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Analyse Chemical shift assignments and structure of the alpha-crystallin domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N0K
Type: protein
Length: 178 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-crystallin B chain
UniProt: P02511
Pockets: 1 · best druggability 0.35

Structure

solution nmr · 1 distinct chain · 3% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-crystallin B chain	protein	89	3% helix, 51% strand	P02511

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	104	0.35	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 802 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2N0K · Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5 · the same entry in another collection · chain A against A, TM-score 1.00
P02511 · AlphaFold monomer V2.0 prediction for alpha-crystallin B chain (P02511) · a predicted model of the same protein · chain B 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 P02511
Elsewhere: RCSB PDB 2N0K · PDBe 2N0K · UniProt P02511

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