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Crystal structure of a susd homolog (BACOVA_04803) from bacteroides ovatus atcc 8483 at 2.25 a resolution
Analyse Crystal structure of a susd homolog (BACOVA_04803) from bacteroides ovatus atcc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F53
- Type
- protein
- Length
- 996 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Susd homolog
- UniProt
- A7M3W3
- Ligands
- CA, CL
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Susd homolog | protein | 498 | 48% helix, 5% strand | A7M3W3 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.72 | 0.77 | 75 | GOL |
| 2 | 130 | 0.55 | 0.82 | 23 | empty |
| 3 | 141 | 0.55 | 0.81 | 23 | empty |
| 4 | 113 | 0.51 | 0.82 | 30 | GOL |
| 5 | 57 | 0.48 | 0.85 | 20 | GOL |
Interfaces
1 interface between chains.
- A–B · 304 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 34 modified (engineered).
Compared structures
- 4F53 · Crystal structure of a susd homolog (BACOVA_04803) from Bacteroides ovatus ATCC 8483 at… · 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 A7M3W3
- Elsewhere: RCSB PDB 4F53 · PDBe 4F53 · UniProt A7M3W3
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