Research workbench
Osteocalcin from fish argyrosomus regius
Analyse Osteocalcin from fish argyrosomus regius in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VZM
- Type
- protein
- Length
- 126 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Osteocalcin
- UniProt
- Q800Y1
- Ligands
- MG
Structure
x-ray diffraction · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Osteocalcin | protein | 43 | 74% helix, 0% strand | Q800Y1 |
| B | Osteocalcin | protein | 42 | 71% helix, 0% strand | Q800Y1 |
| C | Osteocalcin | protein | 41 | 71% helix, 0% strand | Q800Y1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 8 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- A–B · 252 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 228 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified, 2 disulfide (carboxylation, disulfide).
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 Q800Y1
- Elsewhere: RCSB PDB 1VZM · PDBe 1VZM · UniProt Q800Y1
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