MolNFT v1 · #16759 · protein
Pectate lyase C from erwinia chrysanthemi at pH 4.5 with 30MM CA2+
1O8J: “Pectate lyase C from erwinia chrysanthemi at pH 4.5 with 30MM CA2+”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.30). MolNFT v1 #16759 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1O8J
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectate lyase C
- EC
- 4.2.2.2
- UniProt
- P11073
- Ligands
- CA
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pectate lyase C (EC 4.2.2.2) | protein | 352 | 13% helix, 34% strand | P11073 |
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
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 | 69 | 0.30 | 0.74 | 19 | 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 P11073
- Elsewhere: RCSB PDB 1O8J · PDBe 1O8J · UniProt P11073
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