Research workbench
Crystal structure of acetyl xylan esterase 1 from thermoanaerobacterium sp. JW/SL YS485
Analyse Crystal structure of acetyl xylan esterase 1 from thermoanaerobacterium sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FCY
- Type
- protein
- Length
- 951 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylan esterase 1
- EC
- 3.1.1.72, 3.1.1.41
- UniProt
- O30361
- Ligands
- CA
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Xylan esterase 1 (EC 3.1.1.72, 3.1.1.41) | protein | 317 | 36% helix, 21% strand | O30361 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.72 | 0.76 | 61 | empty |
| 2 | 57 | 0.58 | 0.91 | 25 | empty |
| 3 | 317 | 0.54 | 0.75 | 29 | empty |
| 4 | 145 | 0.46 | 0.77 | 23 | empty |
| 5 | 163 | 0.44 | 0.74 | 27 | empty |
Interfaces
3 interfaces between chains.
- B–C · 936 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 882 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 480 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3FCY · Crystal Structure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 · 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 O30361
- Elsewhere: RCSB PDB 3FCY · PDBe 3FCY · UniProt O30361
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