4M5T: Alpha-crystallin B chain

Disulfide trapped human alphaB crystallin core domain in complex with C-terminal peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Apr 2014.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 3,110
Mol. weight: 44.96 kDa
Released: 9 Apr 2014

Explore 4M5T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4M5T contains 18 α-helices and 38 β-strands across 8 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	97-106	10	2
β-strand	113-123	11	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
α-helix	150	1

Chain B: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	157-159	3	2
β-strand	161-163	3	1

Chains C and G: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	68-70	3	4
β-strand	74-80	7	4
α-helix	86-88	3
β-strand	89-94	6	2
β-strand	97-106	10	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	142-148	7	4
α-helix	149-150	2

Chain D: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	157-158	2	4
α-helix	160	1
β-strand	161-162	2	2

Chain E: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	68-70	3	5
β-strand	74-80	7	5
α-helix	86-88	3
β-strand	89-94	6	6
β-strand	97-107	11	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	142-148	7	5
α-helix	149-150	2

Chain F: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	157-159	3	5
α-helix	160	1
β-strand	161-163	3	6

Chain H: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	157-159	3	7
α-helix	160-161	2
β-strand	162	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-crystallin B chain	A, C, E, G	protein	87	Homo sapiens	P02511 (AlphaFold model)
Alpha-crystallin B chain	B, D, F, H	protein	9	Homo sapiens	P02511 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>4M5T_1 Alpha-crystallin B chain (chains A, C, E, G)
GMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISRCFHRKYRIPA
DVDPLTITSSLSSDGVLTVNGPRKQVS

Sequence of entity 2 (B, D, F, H), FASTA

>4M5T_2 Alpha-crystallin B chain (chains B, D, F, H)
ERTIPITRE

Primary citation

The structured core domain of alpha B-crystallin can prevent amyloid fibrillation and associated toxicity. Hochberg, G.K., Ecroyd, H., Liu, C. et al. Proc Natl Acad Sci U S A (2014) 111:E1562-E1570. DOI 10.1073/pnas.1322673111 · 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)
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
3SGN 2.81 Å, Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100

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