Research workbench
Crystal structure of transaldolase (YP_208650.1) from neisseria gonorrhoeae fa 1090 at 1.14 a resolution
Analyse Crystal structure of transaldolase (YP_208650.1) from neisseria gonorrhoeae fa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CLM
- 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
- Q5F6E9
- Ligands
- CL, SO4
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transaldolase (EC 2.2.1.2) | protein | 352 | 58% helix, 11% strand | Q5F6E9 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 11 copies · chains A
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 | 174 | 0.49 | 0.77 | 30 | CL, SO4, EDO |
| 2 | 114 | 0.37 | 0.74 | 19 | EDO |
| 3 | 67 | 0.33 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3CLM · Crystal structure of transaldolase (YP_208650.1) from Neisseria gonorrhoeae FA 1090 at… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5F6E9 · AlphaFold monomer V2.0 prediction for transaldolase (Q5F6E9) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q5F6E9
- Elsewhere: RCSB PDB 3CLM · PDBe 3CLM · UniProt Q5F6E9
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