Research workbench
Identification of zinc ions in LMO4.
Analyse Identification of zinc ions in LMO4. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9F5B
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens
- Molecule
- LIM domain transcription factor LMO4,LIM domain-binding protein 1
- UniProt
- P61968, Q86U70
- Ligands
- ZN
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 15% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LIM domain transcription factor LMO4,LIM domain-binding protein 1 | protein | 166 | 15% helix, 34% strand | P61968, 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.
Compared structures
- P61968 · AlphaFold monomer V2.0 prediction for lim domain transcription factor LMO4 (P61968) · a predicted model of the same protein · chain A against A, TM-score 0.79
- Q86U70 · AlphaFold monomer V2.0 prediction for lim domain-binding protein 1 (Q86U70) · a predicted model of the same protein · chain A 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 P61968
- Every structure of UniProt Q86U70
- Elsewhere: RCSB PDB 9F5B · PDBe 9F5B · UniProt P61968 · UniProt Q86U70
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