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Human alphab crystallin acd R120G
Analyse Human alphab crystallin acd R120G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Y1Z
- Type
- protein
- Length
- 172 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-crystallin B chain
- UniProt
- P02511
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-crystallin B chain | protein | 85 | 7% helix, 56% strand | P02511 |
| B | Alpha-crystallin B chain | protein | 87 | 7% helix, 61% strand | P02511 |
Ligands and binding sites
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 3 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1031 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 2Y1Z · PDBe 2Y1Z · UniProt P02511
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