2Y22: Human AlphaB-crystallin Domain

Human AlphaB-crystallin Domain (residues 67-157). Determined by X-ray diffraction at 3.7 Å resolution. Released 2 Mar 2011.

Method: X-ray diffraction
Resolution: 3.7 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 3,342
Mol. weight: 65.33 kDa
Released: 2 Mar 2011

Explore 2Y22 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y22 contains 14 α-helices and 45 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	68-70	3	1
β-strand	74-80	7	1
α-helix	86-88	3
β-strand	89-94	6	2
β-strand	97-108	12	2
β-strand	113-123	11	2
α-helix	124-125	2
β-strand	128	1	3
α-helix	130-132	3
β-strand	134-137	4	1
β-strand	142-148	7	1
β-strand	149	1	3

Chain B: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	75-80	6	4
β-strand	89-94	6	2
β-strand	97-103	7	2
β-strand	107-108	2	2
β-strand	113-123	11	2
α-helix	124-125	2
α-helix	130-132	3
β-strand	134-137	4	4
β-strand	142-147	6	4

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	76-80	5	5
α-helix	86-88	3
β-strand	89-94	6	6
β-strand	97-103	7	6
β-strand	107-108	2	6
β-strand	113-123	11	6
α-helix	124-125	2
α-helix	130-132	3
β-strand	134-137	4	5
β-strand	142-146	5	5

Chain D: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	70	1	7
β-strand	75-80	6	7
β-strand	89-94	6	6
β-strand	97-103	7	6
β-strand	107-108	2	6
β-strand	113-123	11	6
α-helix	124-125	2
α-helix	130-132	3
β-strand	134-137	4	7
β-strand	142-147	6	7

Chain E: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	74-80	7	8
β-strand	89-94	6	9
β-strand	97-103	7	9
β-strand	107-108	2	9
β-strand	113-123	11	9
α-helix	124-125	2
α-helix	130-132	3
β-strand	134-137	4	8
β-strand	142-148	7	8

Chain F: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	77-80	4	10
β-strand	89-94	6	9
β-strand	97-103	7	9
β-strand	107-108	2	9
β-strand	113-123	11	9
α-helix	124-125	2
α-helix	130-132	3
β-strand	134-137	4	10
β-strand	142-146	5	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-crystallin B	A, B, C, D, E, F	protein	94	HOMO SAPIENS	P02511 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>2Y22_1 ALPHA-CRYSTALLIN B (chains A, B, C, D, E, F)
GAMEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYR
IPADVDPLTITSSMSSDGVLTVNGPRKQVSGPER

Primary citation

Crystal Structure of R120G Disease Mutant of Human Alphab-Crystallin Domain Dimer Shows Closure of a Groove. Clark, A.R., Naylor, C.E., Bagneris, C. et al. J Mol Biol (2011) 408:118. DOI 10.1016/J.JMB.2011.02.020 · PubMed

Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4M5S 1.37 Å, Human alphaB crystallin core domain in complex with C-terminal peptide
3SGP 1.4 Å, Amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L
7ROJ 1.6 Å, Amyloid-related segment of alphaB-crystallin residues 90-100 with G95W mutation
3SGM 1.7 Å, Bromoderivative-2 of amyloid-related segment of alphaB-crystallin residues 90-100
3SGS 1.7 Å, Amyloid-related segment of alphaB-crystallin residues 95-100
2Y1Y 2.0 Å, Human alphaB crystallin ACD(residues 71-157)
4M5T 2.0 Å, Disulfide trapped human alphaB crystallin core domain in complex with C-terminal peptide
3SGR 2.17 Å, Tandem repeat of amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L
2Y1Z 2.5 Å, Human alphaB Crystallin ACD R120G
3SGO 2.56 Å, Amyloid-related segment of alphaB-crystallin residues 90-100
2WJ7 2.63 Å, human alphaB crystallin
5VVV 2.8 Å, Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

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