MolNFT v1 · #120216 · protein
Structural basis of the specific activity and thermostability of pectate lyase (peln) from paenibacillus sp. 0602
5GT5: “Structural basis of the specific activity and thermostability of pectate lyase (peln) from paenibacillus sp.…”. X-ray diffraction, 5 pockets (best druggability 0.66). MolNFT v1 #120216 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5GT5
- Type
- protein
- Length
- 888 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectate lyase
- EC
- 4.2.2.2
- UniProt
- W8CR80
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pectate lyase (EC 4.2.2.2) | protein | 444 | 20% helix, 28% strand | W8CR80 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.66 | 0.84 | 42 | empty |
| 2 | 126 | 0.47 | 0.79 | 20 | empty |
| 3 | 162 | 0.45 | 0.75 | 29 | empty |
| 4 | 65 | 0.35 | 0.77 | 16 | empty |
| 5 | 51 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 612 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5GT5 · Structural basis of the specific activity and thermostability of pectate lyase (pelN)… · 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 W8CR80
- Elsewhere: RCSB PDB 5GT5 · PDBe 5GT5 · UniProt W8CR80
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.