Research workbench
Mad structure of the periplasmique domain of the escherichia COLI pal protein
Analyse Mad structure of the periplasmique domain of the escherichia COLI pal protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OAP
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan-associated lipoprotein
- UniProt
- P07176
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan-associated lipoprotein | protein | 108 | 42% helix, 17% strand | P07176 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1OAP · Mad structure of the periplasmique domain of the Escherichia coli PAL protein · 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 P07176
- Elsewhere: RCSB PDB 1OAP · PDBe 1OAP · UniProt P07176
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