Research workbench
Structure of a CA+2 dependent phosphatidylinositol-specific phospholipase C (pi-plc) enzyme from streptomyces antibioticus
Analyse Structure of a CA+2 dependent phosphatidylinositol-specific phospholipase C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H4W
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-specific phospholipase C1
- EC
- 3.1.4.11
- UniProt
- B3A043
- Ligands
- ACE, CL
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol-specific phospholipase C1 (EC 3.1.4.11) | protein | 315 | 37% helix, 17% strand | B3A043 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- EOH · Ethanol · additive · 8 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3H4W · Structure of a Ca+2 dependent Phosphatidylinositol-specific phospholipase C (PI-PLC)… · 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 B3A043
- Elsewhere: RCSB PDB 3H4W · PDBe 3H4W · UniProt B3A043
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