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The solution structure of reduced dimeric copper zinc sod: the structural effects of dimerization
Analyse The solution structure of reduced dimeric copper zinc sod: the structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L3N
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- CU1, ZN
- Pockets
- 3 · best druggability 0.60
Structure
solution nmr · 1 distinct chain · 2% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 2% helix, 34% strand | P00441 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.60 | 0.78 | 34 | empty |
| 2 | 192 | 0.51 | 0.77 | 25 | empty |
| 3 | 97 | 0.39 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 684 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1L3N · The Solution Structure of Reduced Dimeric Copper Zinc SOD: the Structural Effects of… · 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 P00441
- Elsewhere: RCSB PDB 1L3N · PDBe 1L3N · UniProt P00441
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