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Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A mutant) from amycolatopsis mediterranei (AMGH128_I) in complex with laminaripentaose
Analyse Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UAS
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase
- UniProt
- G0FQ07
- Ligands
- BGC, GLC, ZN
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase | protein | 241 | 36% helix, 20% strand | G0FQ07 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 5 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- ZN · Zinc ion · metal · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UAS · Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A mutant) 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 G0FQ07
- Elsewhere: RCSB PDB 6UAS · PDBe 6UAS · UniProt G0FQ07
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