Research workbench
Crystal structure of the R3 form of pectate lyase a, erwinia chrysanthemi
Analyse Crystal structure of the R3 form of pectate lyase a, erwinia chrysanthemi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JRG
- Type
- protein
- Length
- 704 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectate lyase
- EC
- 4.2.2.2
- UniProt
- P29155
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pectate lyase (EC 4.2.2.2) | protein | 354 | 12% helix, 36% strand | P29155 |
| B | Pectate lyase (EC 4.2.2.2) | protein | 350 | 12% helix, 36% strand | P29155 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
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 | 201 | 0.46 | 0.74 | 47 | SO4 |
| 2 | 74 | 0.31 | 0.74 | 17 | empty |
Compared structures
- 1JRG · Crystal Structure of the R3 form of Pectate Lyase A, Erwinia chrysanthemi · 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 P29155
- Elsewhere: RCSB PDB 1JRG · PDBe 1JRG · UniProt P29155
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