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The crystal structure of TP34 bound to co (II) ion at pH 7.5
Analyse The crystal structure of TP34 bound to co (II) ion at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PJL
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 34 kda membrane antigen
- UniProt
- P19478
- Ligands
- CO, SO4
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 34 kda membrane antigen | protein | 157 | 4% helix, 46% strand | P19478 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 7 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.44 | 0.75 | 32 | empty |
| 2 | 172 | 0.44 | 0.74 | 33 | empty |
| 3 | 74 | 0.38 | 0.78 | 19 | EDO |
| 4 | 65 | 0.36 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1721 Ų buried · 30 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 P19478
- Elsewhere: RCSB PDB 3PJL · PDBe 3PJL · UniProt P19478
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