Research workbench
High resolution structure of penicillium chrysogenum alpha-L- arabinanase
Analyse High resolution structure of penicillium chrysogenum alpha-L- arabinanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A71
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exo-arabinanase
- EC
- 3.2.1.55
- UniProt
- Q7ZA77
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-arabinanase (EC 3.2.1.55) | protein | 353 | 2% helix, 46% strand | Q7ZA77 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.63 | 0.78 | 32 | empty |
| 2 | 245 | 0.57 | 0.78 | 32 | ACT, MPD |
Compared structures
- 3A71 · High resolution structure of Penicillium chrysogenum alpha-L-arabinanase · 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 Q7ZA77
- Elsewhere: RCSB PDB 3A71 · PDBe 3A71 · UniProt Q7ZA77
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