Research workbench
Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A
Analyse Monomeric human CU,ZN superoxide dismutase, loops IV and VII deleted, apo form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XCR
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 110 | 0% helix, 54% strand | P00441 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.41 | 0.76 | 18 | empty |
| 2 | 140 | 0.38 | 0.73 | 23 | empty |
| 3 | 73 | 0.35 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 443 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4XCR · Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant… · 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 4XCR · PDBe 4XCR · UniProt P00441
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