Research workbench
Structural analysis of the microcephaly protein cpap G-box domain suggests a role in centriole elongation.
Analyse Structural analysis of the microcephaly protein cpap G-box domain suggests a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LD1
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- E7FCY1
- Ligands
- NO3
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 157 | 0% helix, 46% strand | E7FCY1 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 2 copies · chains A
- PGE · Triethylene glycol · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4LD1 · Structural analysis of the microcephaly protein CPAP G-box domain suggests a role in… · the same entry in another collection · chain A against A, TM-score 1.00
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 E7FCY1
- Elsewhere: RCSB PDB 4LD1 · PDBe 4LD1 · UniProt E7FCY1
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