Glucuronoarabinoxylan endo-1,4-beta-xylanase
Anaerobacterium chartisolvens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 4 FMT FORMIC ACID × 1 ACY ACETIC ACID × 2 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain B； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 5 FMT FORMIC ACID × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
| 3 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain C； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 6 FMT FORMIC ACID × 2 ACY ACETIC ACID × 2 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
| 4 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain D； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 3 FMT FORMIC ACID × 4 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
| 5 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain E； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 3 FMT FORMIC ACID × 2 ACY ACETIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
| 6 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain F； UniProt 30–450 | Fragment：;The C-terminal was truncated by removing two non-catalytic domains. These removed domains inlcude a carbohydrate binding module family 6 and dockerin domains. ; | GOL GLYCEROL × 1 FMT FORMIC ACID × 2 ACY ACETIC ACID × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.6；289 K；0.17 M ammonium acetate, 0.085 M sodium acetate HCl pH 4.6, 25.5 percent PEG 4000 and 15 percent glycerol | Resolution 1.92 Å R-free 0.205 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
No other PDB entry for the same UniProt protein was found.
View Construct and Data Evidence
| UniProt name | A0A369AIV8_9FIRM |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 26–446； UniProt 30–450 Author chain B； PDBConstruct 26–446； UniProt 30–450 Author chain C； PDBConstruct 26–446； UniProt 30–450 Author chain D； PDBConstruct 26–446； UniProt 30–450 Author chain E； PDBConstruct 26–446； UniProt 30–450 Author chain F； PDBConstruct 26–446； UniProt 30–450 |
