Research workbench
Structural genomics, the crystal structure of a conserved putative domain from neisseria meningitidis MC58
Analyse Structural genomics, the crystal structure of a conserved putative domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O3G
- Type
- protein
- Length
- 76 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative protein
- UniProt
- Q9JYP7
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative protein | protein | 76 | 17% helix, 36% strand | Q9JYP7 |
Ligands and binding sites
- EDO · 1,2-ethanediol · 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: 1 modified (engineered).
Compared structures
- 2O3G · Structural Genomics, the crystal structure of a conserved putative domain from Neisseria… · 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 Q9JYP7
- Elsewhere: RCSB PDB 2O3G · PDBe 2O3G · UniProt Q9JYP7
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