Research workbench
Annexin XII E105K homohexamer crystal structure
Analyse Annexin XII E105K homohexamer crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DM5
- Type
- protein
- Length
- 1,890 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin XII E105K mutant homohexamer
- UniProt
- P26256
- Ligands
- CA
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Annexin XII E105K mutant homohexamer | protein | 315 | 73% helix, 0% strand | P26256 |
Ligands and binding sites
- CA · Calcium ion · metal · 11 copies · chains A, E, B, D, C, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 990 | 0.79 | 0.81 | 102 | CA |
| 2 | 975 | 0.78 | 0.81 | 97 | CA |
| 3 | 751 | 0.77 | 0.82 | 65 | empty |
| 4 | 897 | 0.77 | 0.80 | 97 | empty |
| 5 | 931 | 0.76 | 0.79 | 81 | empty |
Interfaces
12 interfaces between chains.
- A–E · 1071 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1066 Ų buried · 17 hydrogen bonds · protein-protein
- C–F · 1042 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 680 Ų buried · 13 hydrogen bonds · protein-protein
- D–F · 649 Ų buried · 15 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 P26256
- Elsewhere: RCSB PDB 1DM5 · PDBe 1DM5 · UniProt P26256
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