Research workbench
Crystal structure of pud-1/PUD-2 heterodimer
Analyse Crystal structure of pud-1/PUD-2 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JDE
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein F15E11.13; Protein F15E11.1
- UniProt
- G5EET8, G5EBF3
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein F15E11.13 | protein | 144 | 2% helix, 61% strand | G5EET8 |
| B | Protein F15E11.1 | protein | 143 | 2% helix, 59% strand | G5EBF3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1103 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4JDE · Crystal structure of PUD-1/PUD-2 heterodimer · the same entry in another collection · 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 G5EET8
- Every structure of UniProt G5EBF3
- Elsewhere: RCSB PDB 4JDE · PDBe 4JDE · UniProt G5EET8 · UniProt G5EBF3
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