MolNFT v1 · #15956 · protein
Rhamnogalacturonan lyase from aspergillus aculeatus
1NKG · Rhamnogalacturonase B: “Rhamnogalacturonan lyase from aspergillus aculeatus”. X-ray diffraction, 2 ligands (CA, SO4), 4 pockets (best druggability 0.52). MolNFT v1 #15956 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NKG
- Type
- protein
- Length
- 508 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhamnogalacturonase B
- EC
- 4.2.2.-
- UniProt
- Q00019
- Ligands
- CA, SO4
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhamnogalacturonase B (EC 4.2.2.-) | protein | 508 | 7% helix, 44% strand | Q00019 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.52 | 0.77 | 31 | empty |
| 2 | 148 | 0.48 | 0.78 | 24 | empty |
| 3 | 65 | 0.32 | 0.76 | 17 | empty |
| 4 | 50 | 0.25 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q00019
- Elsewhere: RCSB PDB 1NKG · PDBe 1NKG · UniProt Q00019
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