Research workbench
Crystal structure of efb-C from staphylococcus aureus
Analyse Crystal structure of efb-C from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GOM
- Type
- protein
- Length
- 121 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrinogen-binding protein
- UniProt
- P68798
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibrinogen-binding protein | protein | 61 | 85% helix, 3% strand | P68798 |
| B | Fibrinogen-binding protein | protein | 60 | 80% helix, 3% strand | P68798 |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2GOM · Crystal structure of Efb-C from Staphylococcus aureus · 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 P68798
- Elsewhere: RCSB PDB 2GOM · PDBe 2GOM · UniProt P68798
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