Research workbench
Crystal structure of the putative acetylxylan esterase from clostridium acetobutylicum, northeast structural genomics target CAR6
Analyse Crystal structure of the putative acetylxylan esterase from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZMB
- Type
- protein
- Length
- 1,704 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylxylan esterase related enzyme
- UniProt
- Q97LM8
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Acetylxylan esterase related enzyme | protein | 284 | 43% helix, 15% strand | Q97LM8 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.84 | 0.98 | 23 | empty |
| 2 | 186 | 0.83 | 0.98 | 26 | empty |
| 3 | 180 | 0.83 | 0.98 | 24 | empty |
| 4 | 1042 | 0.78 | 0.80 | 94 | empty |
| 5 | 500 | 0.65 | 0.76 | 51 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1857 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1850 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1829 Ų buried · 24 hydrogen bonds · protein-protein
- B–F · 542 Ų buried · 8 hydrogen bonds · protein-protein
- D–F · 146 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 60 modified (engineered).
Compared structures
- 1ZMB · Crystal Structure of the Putative Acetylxylan Esterase from Clostridium acetobutylicum… · 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 Q97LM8
- Elsewhere: RCSB PDB 1ZMB · PDBe 1ZMB · UniProt Q97LM8
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