Research workbench
Refined structure of baboon alpha-lactalbumin at 1.7 ångströms resolution. comparison with C-type lysozyme
Analyse Refined structure of baboon alpha-lactalbumin at 1.7 ångströms resolution.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ALC
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lactalbumin
- UniProt
- P12065
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-lactalbumin | protein | 122 | 45% helix, 10% strand | P12065 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1ALC · Refined structure of baboon alpha-lactalbumin at 1.7 ångströms resolution. comparison… · the same entry in another collection · chain A against A, TM-score 1.00
- P12065 · AlphaFold monomer V2.0 prediction for alpha-lactalbumin (P12065) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P12065
- Elsewhere: RCSB PDB 1ALC · PDBe 1ALC · UniProt P12065
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