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Crystal structure of endoglucanase (TM1049) from thermotoga maritima at 2.01 a resolution
Analyse Crystal structure of endoglucanase (TM1049) from thermotoga maritima at 2.01 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FVG
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- UniProt
- Q9X0D9
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase | protein | 311 | 27% helix, 31% strand | Q9X0D9 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.54 | 0.81 | 23 | EDO |
| 2 | 78 | 0.36 | 0.77 | 14 | EDO |
| 3 | 76 | 0.35 | 0.76 | 23 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 2FVG · Crystal structure of Endoglucanase (tm1049) from THERMOTOGA MARITIMA at 2.01 A resolution · 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 Q9X0D9
- Elsewhere: RCSB PDB 2FVG · PDBe 2FVG · UniProt Q9X0D9
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