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Crystal structure of podospora anserina GH26-CBM35 beta-(1,4)- mannanase
Analyse Crystal structure of podospora anserina GH26-CBM35 beta-(1,4)- mannanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZM8
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GH26 endo-beta-1,4-mannanase
- EC
- 3.2.1.78
- UniProt
- E2GHW2
- Ligands
- NAG, CA, HG
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GH26 endo-beta-1,4-mannanase (EC 3.2.1.78) | protein | 444 | 29% helix, 27% strand | E2GHW2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- CA · Calcium ion · metal · chains A
- HG · Mercury (II) ion · metal · chains A
- TLA · L(+)-tartaric acid · 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 | 126 | 0.39 | 0.74 | 26 | TLA |
| 2 | 58 | 0.29 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 1 glycan (N-glycosylation).
Compared structures
- 3ZM8 · Crystal structure of Podospora anserina GH26-CBM35 beta-(1,4)- mannanase · 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 E2GHW2
- Elsewhere: RCSB PDB 3ZM8 · PDBe 3ZM8 · UniProt E2GHW2
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