Research workbench
Crystal structure of efeo-like protein ALGP7 in complex with a metal ion
Analyse Crystal structure of efeo-like protein ALGP7 in complex with a metal ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y4C
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate-binding protein
- UniProt
- Q25C86
- Ligands
- CU
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alginate-binding protein | protein | 249 | 79% helix, 1% strand | Q25C86 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.35 | 0.75 | 16 | GOL |
Compared structures
- 5Y4C · Crystal structure of EfeO-like protein Algp7 in complex with a metal ion · the same entry in another collection · chain A against A, TM-score 1.00
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 Q25C86
- Elsewhere: RCSB PDB 5Y4C · PDBe 5Y4C · UniProt Q25C86
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