2YGD: Alpha-crystallin B chain
Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach. Determined by electron microscopy at 9.4 Å resolution. Released 7 Dec 2011.
- Method
- Electron microscopy
- Resolution
- 9.4 Å
- Organism
- HOMO SAPIENS
- Chains
- 24
- Atoms
- 34,296
- Mol. weight
- 484.61 kDa
- Released
- 7 Dec 2011
Explore 2YGD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2YGD contains 120 α-helices and 212 β-strands across 24 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.
Chains A and M: 4 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 1 |
| α-helix | 8-14 | 7 | |
| α-helix | 21-24 | 4 | |
| β-strand | 29 | 1 | 2 |
| β-strand | 48 | 1 | 3 |
| α-helix | 52-59 | 8 | |
| β-strand | 73-79 | 7 | 4 |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 97-109 | 13 | 5 |
| β-strand | 112-122 | 11 | 5 |
| β-strand | 134-137 | 4 | 4 |
| β-strand | 143-148 | 6 | 4 |
| α-helix | 167-171 | 5 | |
Chains B, F, H, L, N, R, T and X: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-11 | 5 | |
| α-helix | 12-14 | 3 | |
| α-helix | 22-25 | 4 | |
| β-strand | 29-30 | 2 | 1 |
| β-strand | 40 | 1 | 6 |
| β-strand | 43 | 1 | 6 |
| β-strand | 45 | 1 | 3 |
| α-helix | 53-56 | 4 | |
| α-helix | 60-62 | 3 | |
| β-strand | 74-80 | 7 | 7 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 97-109 | 13 | 5 |
| β-strand | 112-123 | 12 | 5 |
| β-strand | 134-138 | 5 | 7 |
| β-strand | 142-148 | 7 | 7 |
Chains C, I, O and U: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 8 |
| α-helix | 8-14 | 7 | |
| α-helix | 21-24 | 4 | |
| α-helix | 52-59 | 8 | |
| β-strand | 73-79 | 7 | 9 |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 97-109 | 13 | 5 |
| β-strand | 112-122 | 11 | 5 |
| β-strand | 134-137 | 4 | 9 |
| β-strand | 143-148 | 6 | 9 |
| α-helix | 167-171 | 5 | |
Chains D, J, P and V: 6 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-11 | 5 | |
| α-helix | 12-14 | 3 | |
| α-helix | 22-25 | 4 | |
| β-strand | 29-30 | 2 | 8 |
| β-strand | 40 | 1 | 10 |
| β-strand | 43 | 1 | 10 |
| α-helix | 53-56 | 4 | |
| α-helix | 60-62 | 3 | |
| β-strand | 74-80 | 7 | 11 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 97-109 | 13 | 5 |
| β-strand | 112-123 | 12 | 5 |
| β-strand | 134-138 | 5 | 11 |
| β-strand | 142-148 | 7 | 11 |
Chains E and Q: 4 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 12 |
| α-helix | 8-14 | 7 | |
| α-helix | 21-24 | 4 | |
| β-strand | 41 | 1 | 13 |
| β-strand | 48 | 1 | 14 |
| α-helix | 52-59 | 8 | |
| β-strand | 73-79 | 7 | 15 |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 97-109 | 13 | 5 |
| β-strand | 112-122 | 11 | 5 |
| β-strand | 134-137 | 4 | 15 |
| β-strand | 143-148 | 6 | 15 |
| α-helix | 167-171 | 5 | |
Chains G, K, S and W: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 18 |
| α-helix | 8-14 | 7 | |
| α-helix | 21-24 | 4 | |
| β-strand | 48 | 1 | 19 |
| α-helix | 52-59 | 8 | |
| β-strand | 73-79 | 7 | 20 |
| β-strand | 89-94 | 6 | 21 |
| β-strand | 97-109 | 13 | 21 |
| β-strand | 112-122 | 11 | 21 |
| β-strand | 134-137 | 4 | 20 |
| β-strand | 143-148 | 6 | 20 |
| α-helix | 167-171 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Alpha-crystallin B chain | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | protein | 175 | HOMO SAPIENS | P02511 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X), FASTA
>2YGD_1 ALPHA-CRYSTALLIN B CHAIN (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X)
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSW
FDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHR
KYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Primary citation
Multiple Molecular Architectures of the Eye Lens Chaperone Alpha Beta-Crystallin Elucidated by a Triple Hybrid Approach. Braun, N., Zacharias, M., Peschek, J. et al. Proc Natl Acad Sci U S A (2011) 108:20491. DOI 10.1073/PNAS.1111014108 · 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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