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Crystal structure of pectate lyase BSP165PELA from bacillus sp. N165 in complex with trigalacturonate
Analyse Crystal structure of pectate lyase BSP165PELA from bacillus sp. N165 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VMW
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectate lyase
- EC
- 4.2.2.2
- UniProt
- D0VP31
- Ligands
- ADA, SO4
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pectate lyase (EC 4.2.2.2) | protein | 324 | 9% helix, 41% strand | D0VP31 |
Ligands and binding sites
- ADA · alpha-D-galactopyranuronic acid · sugar · 3 copies · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3VMW · Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with… · 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 D0VP31
- Elsewhere: RCSB PDB 3VMW · PDBe 3VMW · UniProt D0VP31
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