MolNFT v1 · #22616 · protein
The crystal structure of triacylglycerol lipase from pseudomonas glumae reveals a partially redundant catalytic aspartate
1TAH: “The crystal structure of triacylglycerol lipase from pseudomonas glumae reveals a partially redundant…”. X-ray diffraction, 1 ligand (CA), 8 pockets (best druggability 0.76). MolNFT v1 #22616 on GenesisL1: 3D structure, binding…
- PDB
- 1TAH
- Type
- protein
- Length
- 1,272 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- Q05489
- Ligands
- CA
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | Lipase (EC 3.1.1.3) | protein | 318 | 38% helix, 17% strand | Q05489 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains B, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.76 | 0.80 | 97 | empty |
| 2 | 662 | 0.71 | 0.78 | 91 | empty |
| 3 | 108 | 0.47 | 0.80 | 26 | empty |
| 4 | 116 | 0.45 | 0.78 | 19 | empty |
| 5 | 50 | 0.44 | 0.84 | 18 | empty |
Interfaces
5 interfaces between chains.
- B–A · 568 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 524 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 370 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 160 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 123 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TAH · The crystal structure of triacylglycerol lipase from pseudomonas glumae reveals a… · the same entry in another collection · chain B against B, 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 1TAH · PDBe 1TAH · UniProt Q05489
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