Research workbench
Crystal structure of the first fibronectin domain of human NCAM1
Analyse Crystal structure of the first fibronectin domain of human NCAM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HAZ
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neural cell adhesion molecule 1
- UniProt
- P13592
- Ligands
- NA
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neural cell adhesion molecule 1 | protein | 104 | 7% helix, 45% strand | P13592 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2HAZ · Crystal structure of the first fibronectin domain of human NCAM1 · 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 P13592
- Elsewhere: RCSB PDB 2HAZ · PDBe 2HAZ · UniProt P13592
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