Research workbench
R. flavefaciens' third scab cohesin in complex with a group 1 dockerin
Analyse R. flavefaciens' third scab cohesin in complex with a group 1 dockerin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M2O
- Type
- protein
- Length
- 211 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cellulosomal scaffoldin protein; Group I dockerin
- UniProt
- A0AEF4
- Ligands
- CA
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cellulosomal scaffoldin protein | protein | 137 | 2% helix, 54% strand | A0AEF4 |
| B | Group I dockerin | protein | 74 | 41% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 923 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 5M2O · R. flavefaciens' third ScaB cohesin in complex with a group 1 dockerin · 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 A0AEF4
- Elsewhere: RCSB PDB 5M2O · PDBe 5M2O · UniProt A0AEF4
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