Research workbench
Crystal structure of cobalt-bound na-asp-2
Analyse Crystal structure of cobalt-bound na-asp-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NUI
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ancylostoma secreted protein 2
- UniProt
- J9ULM6
- Ligands
- CO
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ancylostoma secreted protein 2 | protein | 193 | 32% helix, 19% strand | J9ULM6 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · chains A
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 | 85 | 0.33 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 4NUI · Crystal structure of cobalt-bound Na-ASP-2 · 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 J9ULM6
- Elsewhere: RCSB PDB 4NUI · PDBe 4NUI · UniProt J9ULM6
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