Research workbench
The structure of pentameric human serum amyloid P component
Analyse The structure of pentameric human serum amyloid P component in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SAC
- Type
- protein
- Length
- 1,020 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum amyloid P component
- UniProt
- P02743
- Ligands
- CA
- Pockets
- 4 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Serum amyloid P component | protein | 204 | 5% helix, 46% strand | P02743 |
Ligands and binding sites
- CA · Calcium ion · metal · 10 copies · chains A, B, C, D, E
- ACY · Acetic acid · additive · 4 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.31 | 0.74 | 14 | empty |
| 2 | 77 | 0.30 | 0.73 | 19 | empty |
| 3 | 62 | 0.29 | 0.74 | 16 | empty |
| 4 | 55 | 0.27 | 0.73 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–E · 767 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 764 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 763 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 759 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 757 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P02743
- Elsewhere: RCSB PDB 1SAC · PDBe 1SAC · UniProt P02743
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