Research workbench
Crystal structures of bbp from staphylococcus aureus with peptide ligand
Analyse Crystal structures of bbp from staphylococcus aureus with peptide ligand in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CFA
- Type
- protein
- Length
- 672 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q14U76, P02671
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | Q14U76 |
| B | — | protein | 328 | — | Q14U76 |
| D | — | protein | 8 | — | P02671 |
| C | — | protein | 10 | — | P02671 |
Compared structures
- 5CFA · Crystal structures of Bbp from Staphylococcus aureus with peptide ligand · the same entry in another collection · chain C against C, TM-score 1.00
- Q14U76 · AlphaFold monomer V2.0 prediction for bone sialoprotein-binding protein (Q14U76) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P02671 · AlphaFold monomer V2.0 prediction for fibrinogen alpha chain (P02671) · a predicted model of the same protein · chain D against A, TM-score 0.51
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 Q14U76
- Every structure of UniProt P02671
- Elsewhere: RCSB PDB 5CFA · PDBe 5CFA · UniProt Q14U76 · UniProt P02671
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