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X-ray crystallographic protein structure of the glycoside hydrolase family 30 subfamily 8 xylanase, XYN30A, from clostridium acetobutylicum
Analyse X-ray crystallographic protein structure of the glycoside hydrolase family 30… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CXP
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible xylan degradation enzyme (glycosyl hydrolase family 30-like domain and ricin…
- UniProt
- Q97TI2
- Ligands
- NA, CL
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible xylan degradation enzyme (glycosyl hydrolase family 30-like domain and ricin B-like domain) | protein | 387 | 29% helix, 31% strand | Q97TI2 |
Ligands and binding sites
- NA · Sodium ion · metal · 7 copies · chains A
- CL · Chloride ion · ion · 14 copies · chains A
- P6G · Hexaethylene glycol · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5CXP · X-ray crystallographic protein structure of the glycoside hydrolase family 30 subfamily 8… · 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 Q97TI2
- Elsewhere: RCSB PDB 5CXP · PDBe 5CXP · UniProt Q97TI2
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