Research workbench
Crystal structure of cellulase 12A from thermotoga maritima
Analyse Crystal structure of cellulase 12A from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AMH
- Type
- protein
- Length
- 517 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-glucanase
- EC
- 3.2.1.4
- UniProt
- Q60032
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-glucanase (EC 3.2.1.4) | protein | 256 | 9% helix, 58% strand | Q60032 |
| B | Endo-1,4-beta-glucanase (EC 3.2.1.4) | protein | 261 | 9% helix, 57% strand | Q60032 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.64 | 0.84 | 26 | empty |
| 2 | 189 | 0.60 | 0.82 | 27 | empty |
| 3 | 54 | 0.50 | 0.87 | 15 | empty |
| 4 | 161 | 0.50 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 554 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3AMH · crystal structure of cellulase 12A from Thermotoga maritima · 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 Q60032
- Elsewhere: RCSB PDB 3AMH · PDBe 3AMH · UniProt Q60032
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