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Crystal structure of the SH3 domain from a S. cerevisiae hypothetical 40.4 kda protein at 1.39 a resolution
Analyse Crystal structure of the SH3 domain from a S. cerevisiae hypothetical 40.4 kda… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OOT
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical 40.4 kda protein in PES4-HIS2 intergenic region
- UniProt
- P43603
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical 40.4 kda protein in PES4-HIS2 intergenic region | protein | 58 | 5% helix, 48% strand | P43603 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1OOT · Crystal structure of the SH3 domain from a S. cerevisiae hypothetical 40.4 kDa protein at… · the same entry in another collection · chain A against A, TM-score 1.00
- P43603 · AlphaFold monomer V2.0 prediction for las seventeen-binding protein 3 (P43603) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P43603
- Elsewhere: RCSB PDB 1OOT · PDBe 1OOT · UniProt P43603
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