Research workbench
Crystal structure of the alpha-L-arabinofuranosidase PAABF62A from podospora anserina
Analyse Crystal structure of the alpha-L-arabinofuranosidase PAABF62A from podospora… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N4B
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GH62 arabinofuranosidase
- EC
- 3.2.1.55
- UniProt
- E2GHW5
- Ligands
- CA
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GH62 arabinofuranosidase (EC 3.2.1.55) | protein | 319 | 8% helix, 43% strand | E2GHW5 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.49 | 0.79 | 20 | TRS |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4N4B · Crystal Structure of the alpha-L-arabinofuranosidase PaAbf62A from Podospora anserina · 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 E2GHW5
- Elsewhere: RCSB PDB 4N4B · PDBe 4N4B · UniProt E2GHW5
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