MolNFT v1 · #110822 · protein
Crystal structure of the N-terminal domain of CEACAM7
4Y89 · Carcinoembryonic antigen-related cell adhesion molecule 7: “Crystal structure of the N-terminal domain of CEACAM7”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.34). MolNFT v1 #110822 on GenesisL1: 3D structure…
- PDB
- 4Y89
- Type
- protein
- Length
- 434 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carcinoembryonic antigen-related cell adhesion molecule 7
- UniProt
- A0A0A0MTT6
- Ligands
- CL
- Pockets
- 3 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carcinoembryonic antigen-related cell adhesion molecule 7 | protein | 109 | 6% helix, 49% strand | A0A0A0MTT6 |
| C, D | Carcinoembryonic antigen-related cell adhesion molecule 7 | protein | 108 | 8% helix, 49% strand | A0A0A0MTT6 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.34 | 0.75 | 14 | empty |
| 2 | 100 | 0.32 | 0.73 | 24 | empty |
| 3 | 74 | 0.32 | 0.74 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 827 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 811 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 654 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4Y89 · Crystal structure of the N-terminal domain of CEACAM7 · 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 A0A0A0MTT6
- Elsewhere: RCSB PDB 4Y89 · PDBe 4Y89 · UniProt A0A0A0MTT6
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