MolNFT v1 · #69023 · protein
Structure of the C-terminal domain of bacillus subtilis mutl bound to ZN2+
3KDK · DNA mismatch repair protein mutl: “Structure of the C-terminal domain of bacillus subtilis mutl bound to ZN2+”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #69023 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3KDK
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mismatch repair protein mutl
- UniProt
- P49850
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein mutl | protein | 186 | 40% helix, 25% strand | P49850 |
| B | DNA mismatch repair protein mutl | protein | 184 | 43% helix, 26% strand | P49850 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1056 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3KDK · Structure of the C-terminal domain of Bacillus subtilis MutL bound to Zn2+ · the same entry in another collection · chain A against A, TM-score 1.00
- P49850 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein mutl (P49850) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P49850
- Elsewhere: RCSB PDB 3KDK · PDBe 3KDK · UniProt P49850
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