Research workbench
Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
Analyse Structural determinants of peptide-binding orientation and of sequence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SEM
- Type
- protein
- Length
- 129 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sem-5; 10-residue proline-rich peptide from msos (ACE…
- UniProt
- P29355
- Ligands
- ACE
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sem-5 | protein | 58 | 5% helix, 48% strand | P29355 |
| B | Sem-5 | protein | 57 | 5% helix, 49% strand | P29355 |
| C, D | 10-residue proline-rich peptide from msos (ACE- pro-pro-pro-val-pro-pro-arg-arg-arg) | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 395 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 384 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 227 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 1SEM · Structural determinants of peptide-binding orientation and of sequence specificity in SH3… · the same entry in another collection · chain A against A, TM-score 1.00
- P29355 · AlphaFold monomer V2.0 prediction for sex muscle abnormal protein 5 (P29355) · a predicted model of the same protein · chain B 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 P29355
- Elsewhere: RCSB PDB 1SEM · PDBe 1SEM · UniProt P29355
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.