Structure of a family 26 lichenase in complex with noeuromycin. Determined by X-ray diffraction at 1.2 Å resolution. Released 18 Sept 2007.
Explore 2V3G in 3D Show helices and sheets RCSB PDB PDBe
2V3G contains 9 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-14 | 5 | 1 |
| α-helix | 21-31 | 11 | |
| β-strand | 37-43 | 7 | 1 |
| α-helix | 48-60 | 13 | |
| β-strand | 64-70 | 7 | 1 |
| α-helix | 76-80 | 5 | |
| α-helix | 85-98 | 14 | |
| β-strand | 102-106 | 5 | 1 |
| α-helix | 128-144 | 17 | |
| β-strand | 150-152 | 3 | 1 |
| β-strand | 153 | 1 | 2 |
| β-strand | 156-157 | 2 | 1 |
| α-helix | 174-176 | 3 | |
| β-strand | 179 | 1 | 2 |
| β-strand | 180-186 | 7 | 1 |
| α-helix | 200-211 | 12 | |
| β-strand | 218-225 | 8 | 1 |
| α-helix | 232-246 | 15 | |
| β-strand | 250-256 | 7 | 1 |
| β-strand | 259 | 1 | 3 |
| β-strand | 263 | 1 | 3 |
| α-helix | 270-279 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endoglucanase H | A | protein | 283 | CLOSTRIDIUM THERMOCELLUM | P16218 (AlphaFold model) |
>2V3G_1 ENDOGLUCANASE H (chains A) MASNYNSGLKIGAWVGTQPSESAIKSFQELQGRKLDIVHQFINWSTDFSWVRPYADAVYN NGSILMITWEPWEYNTVDIKNGKADAYITRMAQDMKAYGKEIWLRPLHEANGDWYPWAIG YSSRVNTNETYIAAFRHIVDIFRANGATNVKWVFNVNCDNVGNGTSYLGHYPGDNYVDYT SIDGYNWGTTQSWGSQWQSFDQVFSRAYQALASINKPIIIAEFASAEIGGNKARWITEAY NSIRTSYNKVIAAVWFHENKETDWRINSSPEALAAYREAIGAG
| ID | Name | Formula | Copies |
|---|---|---|---|
| BGC | beta-D-glucopyranose | C6 H12 O6 | 1 |
| NOY | (2R,3S,4R,5R)-5-(hydroxymethyl)piperidine-2,3,4-triol | C6 H13 N O4 | 1 |
D-Glucosylated Derivatives of Isofagomine and Noeuromycin and Their Potential as Inhibitors of Beta-Glycoside Hydrolases. Meloncelli, P.J., Gloster, T.M., Money, V.A. et al. To be published.
Other PDB entries of the same protein (UniProt P16218 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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