Research workbench
Human ncam, FN3 domains 1 and 2
Analyse Human ncam, FN3 domains 1 and 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VKW
- Type
- protein
- Length
- 392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neural cell adhesion molecule 1,140 kda isoform
- UniProt
- P13591
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neural cell adhesion molecule 1,140 kda isoform | protein | 197 | 4% helix, 47% strand | P13591 |
| B | Neural cell adhesion molecule 1,140 kda isoform | protein | 195 | 4% helix, 49% strand | P13591 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.73 | 0.76 | 85 | SO4 |
| 2 | 55 | 0.26 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1376 Ų buried · 25 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 P13591
- Elsewhere: RCSB PDB 2VKW · PDBe 2VKW · UniProt P13591
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