Research workbench
Neisseria gonorrhoeae transaldolase, variant K8A
Analyse Neisseria gonorrhoeae transaldolase, variant K8A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BBX
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transaldolase
- EC
- 2.2.1.2
- UniProt
- A0A1D3FXY0
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transaldolase (EC 2.2.1.2) | protein | 352 | 58% helix, 12% strand | A0A1D3FXY0 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.47 | 0.77 | 25 | EDO, CIT |
| 2 | 111 | 0.36 | 0.74 | 24 | empty |
| 3 | 68 | 0.32 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 7BBX · Neisseria gonorrhoeae transaldolase, variant K8A · 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 A0A1D3FXY0
- Elsewhere: RCSB PDB 7BBX · PDBe 7BBX · UniProt A0A1D3FXY0
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