MolNFT v1 · #18105 · protein
Mutations in the T1.5 loop of pectate lyase a
1PE9: “Mutations in the T1.5 loop of pectate lyase a”. X-ray diffraction, 4 pockets (best druggability 0.74). MolNFT v1 #18105 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PE9
- Type
- protein
- Length
- 722 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectate lyase a
- EC
- 4.2.2.2
- UniProt
- P29155
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pectate lyase a (EC 4.2.2.2) | protein | 361 | 13% helix, 36% strand | P29155 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 801 | 0.74 | 0.79 | 68 | empty |
| 2 | 82 | 0.47 | 0.82 | 21 | empty |
| 3 | 190 | 0.47 | 0.75 | 32 | empty |
| 4 | 188 | 0.47 | 0.75 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 546 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1PE9 · Mutations in the T1.5 loop of pectate lyase a · 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 1PE9 · PDBe 1PE9 · UniProt P29155
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.