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Crystal structure of amicyanin substituted with cobalt
Analyse Crystal structure of amicyanin substituted with cobalt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T5K
- Type
- protein
- Length
- 420 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amicyanin
- UniProt
- P22364
- Ligands
- CO, PO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Amicyanin | protein | 105 | 3% helix, 50% strand | P22364 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 566 | 0.72 | 0.80 | 41 | empty |
| 2 | 409 | 0.67 | 0.80 | 37 | empty |
| 3 | 133 | 0.52 | 0.81 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–C · 412 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 293 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 262 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 240 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 240 Ų buried · 7 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 P22364
- Elsewhere: RCSB PDB 1T5K · PDBe 1T5K · UniProt P22364
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