Research workbench
Crystal structure of acetyl xylan esterase (TM0077) from thermotoga maritima at 2.10 a resolution
Analyse Crystal structure of acetyl xylan esterase (TM0077) from thermotoga maritima at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VLQ
- Type
- protein
- Length
- 3,864 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl xylan esterase
- EC
- 3.1.1.41
- UniProt
- Q9WXT2
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Acetyl xylan esterase (EC 3.1.1.41) | protein | 322 | 35% helix, 20% strand | Q9WXT2 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1131 | 0.82 | 0.83 | 107 | empty |
| 2 | 1015 | 0.76 | 0.78 | 92 | empty |
| 3 | 938 | 0.76 | 0.78 | 69 | empty |
| 4 | 884 | 0.75 | 0.78 | 63 | empty |
| 5 | 1135 | 0.74 | 0.77 | 77 | empty |
Interfaces
28 interfaces between chains.
- J–K · 1126 Ų buried · 25 hydrogen bonds · protein-protein
- G–L · 1121 Ų buried · 22 hydrogen bonds · protein-protein
- H–I · 1110 Ų buried · 25 hydrogen bonds · protein-protein
- A–F · 1106 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1101 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 60 modified (engineered).
Compared structures
- 1VLQ · Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A… · the same entry in another collection · chain L against L, 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 Q9WXT2
- Elsewhere: RCSB PDB 1VLQ · PDBe 1VLQ · UniProt Q9WXT2
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