Research workbench
Crystal structure of CU(II)(SAL-PHE)/APO-myoglobin
Analyse Crystal structure of CU(II)(SAL-PHE)/APO-myoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EB8
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P02185
- Ligands
- CUP, PO4
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myoglobin | protein | 154 | 69% helix, 0% strand | P02185 |
Ligands and binding sites
- CUP · (N-salicyliden-L-phenylalanato)-copper(ii) · ligand · chains A
- PO4 · Phosphate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.80 | 0.91 | 33 | CUP |
| 2 | 71 | 0.50 | 0.84 | 19 | empty |
Compared structures
- 2EB8 · Crystal Structure of Cu(II)(Sal-Phe)/apo-Myoglobin · 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 P02185
- Elsewhere: RCSB PDB 2EB8 · PDBe 2EB8 · UniProt P02185
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