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Crystal structure of the protein human CEACAM1
Analyse Crystal structure of the protein human CEACAM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DZL
- Type
- protein
- Length
- 429 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carcinoembryonic antigen-related cell adhesion molecule 1
- UniProt
- P13688
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Carcinoembryonic antigen-related cell adhesion molecule 1 | protein | 107 | 6% helix, 51% strand | P13688 |
| D | Carcinoembryonic antigen-related cell adhesion molecule 1 | protein | 108 | 0% helix, 48% strand | P13688 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1156 | 0.75 | 0.78 | 69 | empty |
| 2 | 167 | 0.49 | 0.77 | 29 | empty |
| 3 | 86 | 0.36 | 0.76 | 20 | empty |
Interfaces
5 interfaces between chains.
- A–B · 859 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 843 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 257 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 238 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 114 Ų buried · 0 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 P13688
- Elsewhere: RCSB PDB 5DZL · PDBe 5DZL · UniProt P13688
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