Research workbench
Amyloid-related segment of alphab-crystallin residues 90-100 mutant V91L
Analyse Amyloid-related segment of alphab-crystallin residues 90-100 mutant V91L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SGP
- Type
- protein
- Length
- 44 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-crystallin B chain
- UniProt
- P02511
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 82% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Alpha-crystallin B chain | protein | 11 | 0% helix, 82% strand | P02511 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B, C, D
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- C–D · 557 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 535 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3SGP · Amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L · the same entry in another collection · chain D against D, TM-score 1.00
- P02511 · AlphaFold monomer V2.0 prediction for alpha-crystallin B chain (P02511) · a predicted model of the same protein · chain D against A, TM-score 0.39
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 3SGP · PDBe 3SGP · UniProt P02511
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