MolNFT v1 · #29867 · protein
Re-evaluation of the low-temperature azide in mn-dependent superoxide dismutase
1ZLZ: “Re-evaluation of the low-temperature azide in mn-dependent superoxide dismutase”. X-ray diffraction, 2 ligands (MH2, AZI), 4 pockets (best druggability 0.49). MolNFT v1 #29867 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1ZLZ
- Type
- protein
- Length
- 410 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P00448
- Ligands
- MH2, AZI
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase (EC 1.15.1.1) | protein | 205 | 57% helix, 12% strand | P00448 |
Ligands and binding sites
- MH2 · Manganese ion, 1 hydroxyl coordinated · ligand · 2 copies · chains A, B
- AZI · Azide ion · ion · 2 copies · chains 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 | 133 | 0.49 | 0.79 | 22 | empty |
| 2 | 138 | 0.48 | 0.78 | 23 | empty |
| 3 | 66 | 0.40 | 0.80 | 20 | empty |
| 4 | 80 | 0.40 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 990 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1ZLZ · Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase · the same entry in another collection · chain A against A, TM-score 1.00
- P00448 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn] (P00448) · a predicted model of the same protein · 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 P00448
- Elsewhere: RCSB PDB 1ZLZ · PDBe 1ZLZ · UniProt P00448
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