Research workbench
Crystal structure of the MK2H_DELTAP peptide homodimer
Analyse Crystal structure of the MK2H_DELTAP peptide homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DXU
- Type
- protein
- Length
- 172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MK2H_DP protein
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | MK2H_DP protein | protein | 43 | 23% helix, 37% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains B, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- B–A · 2296 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 2245 Ų buried · 51 hydrogen bonds · protein-protein
- A–D · 245 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 169 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 141 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7DXU · Crystal structure of the mk2h_deltaP peptide homodimer · the same entry in another collection · chain B against B, 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
- Elsewhere: RCSB PDB 7DXU · PDBe 7DXU
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