MolNFT v1 · #175814 · protein
Tetrameric coiled-coil structure of liprin-ALPHA2_H2
7D2H · Liprin-alpha-2: “Tetrameric coiled-coil structure of liprin-ALPHA2_H2”. X-ray diffraction. MolNFT v1 #175814 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7D2H
- Type
- protein
- Length
- 228 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Liprin-alpha-2
- UniProt
- O75334
Structure
x-ray diffraction · 4 distinct chains · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Liprin-alpha-2 | protein | 57 | 93% helix, 0% strand | O75334 |
| B | Liprin-alpha-2 | protein | 55 | 91% helix, 0% strand | O75334 |
| C | Liprin-alpha-2 | protein | 56 | 95% helix, 0% strand | O75334 |
| D | Liprin-alpha-2 | protein | 60 | 95% helix, 0% strand | O75334 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–B · 1093 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1066 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 725 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 692 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 532 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 O75334
- Elsewhere: RCSB PDB 7D2H · PDBe 7D2H · UniProt O75334
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