Research workbench
Human S-PLA2 in complex with indole 6
Analyse Human S-PLA2 in complex with indole 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DB5
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (phospholipase A2)
- EC
- 3.1.1.4
- UniProt
- P14555
- Ligands
- 6IN, CA
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (phospholipase A2) (EC 3.1.1.4) | protein | 124 | 51% helix, 6% strand | P14555 |
Ligands and binding sites
- 6IN · 4-(1-benzyl-3-carbamoylmethyl-2-methyl-1H-indol-5-yloxy)-butyric acid · ligand · chains A
- CA · Calcium ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.56 | 0.80 | 24 | 6IN |
Modifications
Observed in the structure: 7 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 P14555
- Elsewhere: RCSB PDB 1DB5 · PDBe 1DB5 · UniProt P14555
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