Research workbench
Crystal structure of a putative outer membrane chaperone (omph-like) (CC_1914) from caulobacter crescentus CB15 at 2.83 a resolution (psi community target, shapiro)
Analyse Crystal structure of a putative outer membrane chaperone (omph-like) (CC_1914)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KQT
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative outer membrane chaperone (omph-like)
- UniProt
- Q9A712
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative outer membrane chaperone (omph-like) | protein | 169 | 69% helix, 5% strand | Q9A712 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- PGE · Triethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 4KQT · Crystal structure of a putative outer membrane chaperone (OmpH-like) (CC_1914) from… · 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 Q9A712
- Elsewhere: RCSB PDB 4KQT · PDBe 4KQT · UniProt Q9A712
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.