Research workbench
Structure of wild-type ISL2-lid in complex with LHX4-LIM1+2
Analyse Structure of wild-type ISL2-lid in complex with LHX4-LIM1+2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CME
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LIM/HOMEOBOX protein LHX4,INSULIN gene enhancer protein isl-2
- UniProt
- P53776, Q9CXV0
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | LIM/HOMEOBOX protein LHX4,INSULIN gene enhancer protein isl-2 | protein | 154 | 13% helix, 33% strand | P53776, Q9CXV0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.37 | 0.74 | 19 | empty |
| 2 | 82 | 0.32 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 39 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6CME · Structure of wild-type ISL2-LID in complex with LHX4-LIM1+2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9CXV0 · AlphaFold monomer V2.0 prediction for insulin gene enhancer protein isl-2 (Q9CXV0) · a predicted model of the same protein · chain A against A, TM-score 0.53
- P53776 · AlphaFold monomer V2.0 prediction for LIM/HOMEOBOX protein LHX4 (P53776) · a predicted model of the same protein · chain A against A, TM-score 0.41
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 P53776
- Every structure of UniProt Q9CXV0
- Elsewhere: RCSB PDB 6CME · PDBe 6CME · UniProt P53776 · UniProt Q9CXV0
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