Research workbench
Crystal structure of SE1688 protein from staphylococcus epidermidis. northeast structural genomics consortium target SER89
Analyse Crystal structure of SE1688 protein from staphylococcus epidermidis. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QGS
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein SE1688
- UniProt
- Q8CRP0
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein SE1688 | protein | 209 | 68% helix, 0% strand | Q8CRP0 |
| B | Protein SE1688 | protein | 199 | 69% helix, 0% strand | Q8CRP0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.56 | 0.76 | 43 | ZN |
| 2 | 100 | 0.39 | 0.76 | 17 | empty |
| 3 | 114 | 0.36 | 0.74 | 25 | empty |
| 4 | 72 | 0.36 | 0.77 | 14 | empty |
| 5 | 55 | 0.31 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1733 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2QGS · Crystal structure of SE1688 protein from Staphylococcus epidermidis. Northeast Structural… · 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 Q8CRP0
- Elsewhere: RCSB PDB 2QGS · PDBe 2QGS · UniProt Q8CRP0
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