Research workbench
Outer membrane phospholipase a from escherichia COLI N156A active site mutant pH 6.1
Analyse Outer membrane phospholipase a from escherichia COLI N156A active site mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ILZ
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane phospholipase a
- EC
- 3.1.1.32
- UniProt
- P0A921
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane phospholipase a (EC 3.1.1.32) | protein | 257 | 7% helix, 56% strand | P0A921 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 5 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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 | 296 | 0.73 | 0.86 | 59 | empty |
Compared structures
- 1ILZ · OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1 · the same entry in another collection · chain A against A, TM-score 1.00
- P0A921 · AlphaFold monomer V2.0 prediction for phospholipase A1 (P0A921) · a predicted model of the same protein · 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 P0A921
- Elsewhere: RCSB PDB 1ILZ · PDBe 1ILZ · UniProt P0A921
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