MolNFT v1 · #49315 · protein
Structural and kinetic study of the differences between human and E.COLI manganese superoxide dismutases
2QKC · Superoxide dismutase [mn]: “Structural and kinetic study of the differences between human and E.COLI manganese superoxide dismutases”. X-ray diffraction, 1 ligand (MN). MolNFT v1 #49315 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2QKC
- Type
- protein
- Length
- 392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [mn]
- EC
- 1.15.1.1
- UniProt
- P04179
- Ligands
- MN
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Superoxide dismutase [mn] (EC 1.15.1.1) | protein | 196 | 58% helix, 13% strand | P04179 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 1064 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2QKC · Structural and Kinetic Study of the Differences between Human and E.coli Manganese… · the same entry in another collection · chain A against A, TM-score 1.00
- P04179 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn], mitochondrial (P04179) · 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 P04179
- Elsewhere: RCSB PDB 2QKC · PDBe 2QKC · UniProt P04179
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