Research workbench
Two intramolecular isopeptide bonds are identified in the crystal structure of the streptococcus gordonii sspb C-terminal domain
Analyse Two intramolecular isopeptide bonds are identified in the crystal structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WZA
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agglutinin receptor
- UniProt
- P16952
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agglutinin receptor | protein | 338 | 12% helix, 43% strand | P16952 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 isopeptide (isopeptide).
Compared structures
- 2WZA · Two intramolecular isopeptide bonds are identified in the crystal structure of the… · the same entry in another collection · chain A against A, TM-score 1.00
- P16952 · AlphaFold monomer V2.0 prediction for agglutinin receptor (P16952) · 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 P16952
- Elsewhere: RCSB PDB 2WZA · PDBe 2WZA · UniProt P16952
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