Research workbench
Crystal structure of the tatd-like protein (AF1765) from archaeoglobus fulgidus, northeast structural genomics consortium target GR121
Analyse Crystal structure of the tatd-like protein (AF1765) from archaeoglobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GUW
- Type
- protein
- Length
- 932 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein AF_1765
- UniProt
- O28509
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Uncharacterized protein AF_1765 | protein | 233 | 41% helix, 12% strand | O28509 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.67 | 0.91 | 19 | empty |
| 2 | 94 | 0.66 | 0.91 | 17 | empty |
| 3 | 88 | 0.66 | 0.91 | 20 | empty |
| 4 | 90 | 0.65 | 0.90 | 19 | empty |
| 5 | 352 | 0.59 | 0.76 | 37 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1200 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1199 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 262 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 131 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 3GUW · Crystal Structure of the TatD-like Protein (AF1765) from Archaeoglobus fulgidus… · 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 O28509
- Elsewhere: RCSB PDB 3GUW · PDBe 3GUW · UniProt O28509
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