Research workbench
Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from fusarium oxysporum 12S, H105F rha-glca complex
Analyse Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from fusarium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ESN
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-rhamnose-alpha-1,4-D-glucuronate lyase
- EC
- 4.2.2.-
- Ligands
- BDP, RAM, NAG, SO4
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-rhamnose-alpha-1,4-D-glucuronate lyase (EC 4.2.2.-) | protein | 435 | 3% helix, 46% strand | — |
Ligands and binding sites
- BDP · beta-D-glucopyranuronic acid · sugar · chains A
- RAM · alpha-L-rhamnopyranose · sugar · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.69 | 0.84 | 47 | empty |
| 2 | 194 | 0.52 | 0.78 | 23 | BDP, RAM |
Modifications
Observed in the structure: 1 glycan (N-glycosylation).
Compared structures
- 7ESN · Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from Fusarium oxysporum… · 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
- Elsewhere: RCSB PDB 7ESN · PDBe 7ESN
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