Research workbench
Uncharacterized protein conserved in bacteria, COG3792 from neisseria meningitidis
Analyse Uncharacterized protein conserved in bacteria, COG3792 from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O5H
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9K0R7
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 128 | — | Q9K0R7 |
| B | — | protein | 118 | — | Q9K0R7 |
Compared structures
- 2O5H · Uncharacterized Protein Conserved in Bacteria, COG3792 from Neisseria meningitidis · 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 Q9K0R7
- Elsewhere: RCSB PDB 2O5H · PDBe 2O5H · UniProt Q9K0R7
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