Research workbench
High resolution native crystal structure of an uncharacterized acr, COG1565 superfamily protein from burkholderia thailandensis, solved by iodide ion sad
Analyse High resolution native crystal structure of an uncharacterized acr, COG1565… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F3N
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized acr, COG1565 superfamily
- UniProt
- Q2T1U7
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized acr, COG1565 superfamily | protein | 374 | 39% helix, 23% strand | Q2T1U7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.74 | 0.86 | 42 | EDO |
| 2 | 89 | 0.38 | 0.76 | 15 | empty |
| 3 | 97 | 0.36 | 0.75 | 21 | empty |
Compared structures
- 4F3N · High resolution native crystal structure of an uncharacterized ACR, COG1565 superfamily… · 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 Q2T1U7
- Elsewhere: RCSB PDB 4F3N · PDBe 4F3N · UniProt Q2T1U7
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