MolNFT v1 · #19299 · protein
New crystal form of pseudomonas glumae (formerly chromobacterium viscosum atcc 6918) lipase
1QGE · Protein (triacylglycerol hydrolase): “New crystal form of pseudomonas glumae (formerly chromobacterium viscosum atcc 6918) lipase”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.40). MolNFT v1 #19299 on GenesisL1…
- PDB
- 1QGE
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (triacylglycerol hydrolase)
- EC
- 3.1.1.3
- UniProt
- Q05489
- Ligands
- CA
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Protein (triacylglycerol hydrolase) (EC 3.1.1.3) | protein | 219 | 38% helix, 17% strand | Q05489 |
| E | Protein (triacylglycerol hydrolase) (EC 3.1.1.3) | protein | 97 | 40% helix, 12% strand | Q05489 |
Ligands and binding sites
- CA · Calcium ion · metal · chains E
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 | 61 | 0.40 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- D–E · 3036 Ų buried · 57 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1QGE · New crystal form of pseudomonas glumae (formerly chromobacterium viscosum atcc 6918)… · the same entry in another collection · chain D against D, 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 Q05489
- Elsewhere: RCSB PDB 1QGE · PDBe 1QGE · UniProt Q05489
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