Research workbench
Crystal structure of the LMO2:LDB1-lid complex, P21 crystal form
Analyse Crystal structure of the LMO2:LDB1-lid complex, P21 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XJY
- Type
- protein
- Length
- 166 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhombotin-2; Lim domain-binding protein 1
- UniProt
- P25791, Q86U70
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhombotin-2 | protein | 131 | 17% helix, 34% strand | P25791 |
| B | Lim domain-binding protein 1 | protein | 35 | 0% helix, 29% strand | Q86U70 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1810 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2XJY · Crystal structure of the LMO2:LDB1-LID complex, P21 crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- P25791 · AlphaFold monomer V2.0 prediction for rhombotin-2 (P25791) · a predicted model of the same protein · chain A against A, TM-score 0.83
- Q86U70 · AlphaFold monomer V2.0 prediction for lim domain-binding protein 1 (Q86U70) · a predicted model of the same protein · chain B against A, TM-score 0.30
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 P25791
- Every structure of UniProt Q86U70
- Elsewhere: RCSB PDB 2XJY · PDBe 2XJY · UniProt P25791 · UniProt Q86U70
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