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Crystal structure of the catalytic module of a family 98 glycoside hydrolase from streptococcus pneumoniae TIGR4 in complex with the H- disaccharide blood group antigen.
Analyse Crystal structure of the catalytic module of a family 98 glycoside hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WMH
- Type
- protein
- Length
- 553 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fucolectin-related protein
- UniProt
- Q97N96
- Ligands
- GAL, FUC
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fucolectin-related protein | protein | 553 | 33% helix, 25% strand | Q97N96 |
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 | 239 | 0.58 | 0.78 | 28 | GAL, FUC |
| 2 | 197 | 0.50 | 0.76 | 40 | empty |
| 3 | 62 | 0.32 | 0.76 | 14 | empty |
Compared structures
- 2WMH · Crystal structure of the catalytic module of a family 98 glycoside hydrolase from… · 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 Q97N96
- Elsewhere: RCSB PDB 2WMH · PDBe 2WMH · UniProt Q97N96
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