Research workbench
Solution NMR structure of C2H2-type zinc-fingers 4 and 5 from human insulinoma-associated protein 1 (fragment 424-497), northeast structural genomics consortium target HR7614B
Analyse Solution NMR structure of C2H2-type zinc-fingers 4 and 5 from human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LV2
- Type
- protein
- Length
- 85 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulinoma-associated protein 1
- UniProt
- Q01101
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 24% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulinoma-associated protein 1 | protein | 85 | 24% helix, 9% strand | Q01101 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2LV2 · Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01101 · AlphaFold monomer V2.0 prediction for insulinoma-associated protein 1 (Q01101) · a predicted model of the same protein · chain A against A, TM-score 0.48
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 Q01101
- Elsewhere: RCSB PDB 2LV2 · PDBe 2LV2 · UniProt Q01101
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