Research workbench
Bacillus subtilis pectate lyase R279K mutant
Analyse Bacillus subtilis pectate lyase R279K mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BSP
- Type
- protein
- Length
- 399 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (pectate lyase)
- EC
- 4.2.2.2
- UniProt
- P39116
- Ligands
- CA
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (pectate lyase) (EC 4.2.2.2) | protein | 399 | 19% helix, 30% strand | P39116 |
Ligands and binding sites
- CA · Calcium ion · metal · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.38 | 0.73 | 26 | CA |
| 2 | 97 | 0.35 | 0.74 | 20 | empty |
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 P39116
- Elsewhere: RCSB PDB 2BSP · PDBe 2BSP · UniProt P39116
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