Research workbench
L-rhamnulose-1-phosphate aldolase from escherichia COLI ( mutant E117S-E192A-K248G-R253A-E254A)
Analyse L-rhamnulose-1-phosphate aldolase from escherichia COLI ( mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V2B
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhamnulose-1-phosphate aldolase
- EC
- 4.1.2.19
- UniProt
- P32169
- Ligands
- ZN, PO4
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) | protein | 272 | 45% helix, 17% strand | P32169 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- ACT · Acetate ion · additive · chains A
- PGR · R-1,2-propanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.42 | 0.79 | 21 | empty |
| 2 | 52 | 0.27 | 0.74 | 16 | empty |
Compared structures
- 2V2B · L-rhamnulose-1-phosphate aldolase from escherichia COLI (mutant E117S… · the same entry in another collection · chain A against A, TM-score 1.00
- P32169 · AlphaFold monomer V2.0 prediction for rhamnulose-1-phosphate aldolase (P32169) · 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 P32169
- Elsewhere: RCSB PDB 2V2B · PDBe 2V2B · UniProt P32169
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