Research workbench
High resolution structures of monomeric S. pyogenes speb reveals role of glycine-rich active site loop
Analyse High resolution structures of monomeric S. pyogenes speb reveals role of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D8I
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptopain; ACE-aeik-cho aldehyde (bound form)
- EC
- 3.4.22.10
- UniProt
- E0PTS8
- Ligands
- ACE, NO3
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptopain (EC 3.4.22.10) | protein | 254 | 25% helix, 22% strand | E0PTS8 |
| B | ACE-aeik-cho aldehyde (bound form) | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 336 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 4D8I · High resolution structures of monomeric S. pyogenes SpeB reveals role of glycine-rich… · 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 E0PTS8
- Elsewhere: RCSB PDB 4D8I · PDBe 4D8I · UniProt E0PTS8
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