Research workbench
Crystal structure of an actin depolymerizing factor
Analyse Crystal structure of an actin depolymerizing factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q2B
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- COFILIN/ACTIN-depolymerizing factor homolog 1
- UniProt
- P86292
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | COFILIN/ACTIN-depolymerizing factor homolog 1 | protein | 120 | 35% helix, 30% strand | P86292 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A
- TAR · D(-)-tartaric acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 3Q2B · Crystal Structure of an Actin Depolymerizing Factor · the same entry in another collection · chain A against A, TM-score 1.00
- P86292 · AlphaFold monomer V2.0 prediction for COFILIN/ACTIN-depolymerizing factor homolog 1… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P86292
- Elsewhere: RCSB PDB 3Q2B · PDBe 3Q2B · UniProt P86292
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