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Human alphab crystallin

Analyse Human alphab crystallin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WJ7
Type: protein
Length: 387 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-crystallin B chain
UniProt: P02511
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Alpha-crystallin B chain	protein	85	7% helix, 55% strand	P02511
B	Alpha-crystallin B chain	protein	72	4% helix, 53% strand	P02511
D	Alpha-crystallin B chain	protein	71	4% helix, 59% strand	P02511
E	Alpha-crystallin B chain	protein	74	8% helix, 59% strand	P02511

Pockets

4 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	391	0.64	0.78	28	empty
2	348	0.63	0.78	27	empty
3	272	0.57	0.78	37	empty
4	274	0.55	0.76	38	empty

Interfaces

4 interfaces between chains.

A–B · 746 Å² buried · 21 hydrogen bonds · protein-protein
C–D · 635 Å² buried · 25 hydrogen bonds · protein-protein
D–E · 308 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 304 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2WJ7 · human alphaB crystallin · the same entry in another collection · chain E against E, TM-score 1.00
P02511 · AlphaFold monomer V2.0 prediction for alpha-crystallin B chain (P02511) · a predicted model of the same protein · chain E against A, TM-score 0.96

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 2WJ7 · PDBe 2WJ7 · UniProt P02511

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