Research workbench
Crystal structure of the conserved staphylococcal antigen 1A, CSA1A
Analyse Crystal structure of the conserved staphylococcal antigen 1A, CSA1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BIH
- Type
- protein
- Length
- 678 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized lipoprotein SAOUHSC_00053
- UniProt
- Q2G1Q1
- Ligands
- CA
- Pockets
- 12 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 14% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized lipoprotein SAOUHSC_00053 | protein | 172 | 16% helix, 41% strand | Q2G1Q1 |
| B | Uncharacterized lipoprotein SAOUHSC_00053 | protein | 166 | 14% helix, 42% strand | Q2G1Q1 |
| C | Uncharacterized lipoprotein SAOUHSC_00053 | protein | 177 | 12% helix, 38% strand | Q2G1Q1 |
| D | Uncharacterized lipoprotein SAOUHSC_00053 | protein | 163 | 15% helix, 44% strand | Q2G1Q1 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 769 | 0.71 | 0.77 | 67 | empty |
| 2 | 562 | 0.63 | 0.75 | 54 | empty |
| 3 | 675 | 0.63 | 0.73 | 53 | empty |
| 4 | 122 | 0.44 | 0.77 | 14 | empty |
| 5 | 114 | 0.43 | 0.77 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–D · 348 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 261 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 201 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 141 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 36 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4BIH · Crystal structure of the conserved staphylococcal antigen 1A, Csa1A · the same entry in another collection · chain D against D, TM-score 1.00
- Q2G1Q1 · AlphaFold monomer V2.0 prediction for uncharacterized lipoprotein SAOUHSC_00052 (Q2G1Q1) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q2G1Q1
- Elsewhere: RCSB PDB 4BIH · PDBe 4BIH · UniProt Q2G1Q1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.