Research workbench

Human alphab-crystallin domain (residues 67-157)

Analyse Human alphab-crystallin domain (residues 67-157) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y22
Type: protein
Length: 467 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-crystallin B
UniProt: P02511
Pockets: 6 · best druggability 0.63

Structure

x-ray diffraction · 6 distinct chains · 5% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-crystallin B	protein	86	7% helix, 60% strand	P02511
B	Alpha-crystallin B	protein	76	4% helix, 55% strand	P02511
C	Alpha-crystallin B	protein	74	8% helix, 54% strand	P02511
D	Alpha-crystallin B	protein	80	4% helix, 54% strand	P02511
E	Alpha-crystallin B	protein	77	4% helix, 57% strand	P02511
F	Alpha-crystallin B	protein	74	4% helix, 53% strand	P02511

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	348	0.63	0.79	28	empty
2	362	0.62	0.78	31	empty
3	564	0.62	0.74	63	empty
4	287	0.61	0.79	23	empty
5	58	0.44	0.83	20	empty

Interfaces

6 interfaces between chains.

A–B · 618 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 603 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 588 Å² buried · 23 hydrogen bonds · protein-protein
B–E · 78 Å² buried · 0 hydrogen bonds · protein-protein
D–E · 70 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2Y22 · Human AlphaB-crystallin Domain (residues 67-157) · the same entry in another collection · chain F against F, 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 0.98

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 2Y22 · PDBe 2Y22 · UniProt P02511

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.