Research workbench
Crystal structure of the N terminal domain of human CEACAM1
Analyse Crystal structure of the N terminal domain of human CEACAM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GK2
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carcinoembryonic antigen-related cell adhesion molecule 1
- UniProt
- P13688
- Ligands
- NI
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carcinoembryonic antigen-related cell adhesion molecule 1 | protein | 109 | 6% helix, 50% strand | P13688 |
| B | Carcinoembryonic antigen-related cell adhesion molecule 1 | protein | 111 | 5% helix, 50% strand | P13688 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
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 | 60 | 0.40 | 0.80 | 21 | GOL |
Interfaces
1 interface between chains.
- A–B · 508 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2GK2 · Crystal structure of the N terminal domain of human CEACAM1 · the same entry in another collection · chain A against A, TM-score 1.00
- P13688 · AlphaFold monomer V2.0 prediction for carcinoembryonic antigen- related cell adhesion… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P13688
- Elsewhere: RCSB PDB 2GK2 · PDBe 2GK2 · UniProt P13688
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.