Research workbench
NMB1532 protein from neisseria meningitidis, unknown function
Analyse NMB1532 protein from neisseria meningitidis, unknown function in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P0N
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein NMB1532
- UniProt
- Q9JYL1
- Ligands
- MN, CL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein NMB1532 | protein | 161 | 87% helix, 0% strand | Q9JYL1 |
| B | Hypothetical protein NMB1532 | protein | 158 | 89% helix, 0% strand | Q9JYL1 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.70 | 0.86 | 26 | empty |
| 2 | 132 | 0.40 | 0.74 | 25 | GOL |
| 3 | 60 | 0.33 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 454 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 2 covalent (engineered, additive adduct).
Compared structures
- 2P0N · NMB1532 protein from Neisseria meningitidis, unknown function · 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 Q9JYL1
- Elsewhere: RCSB PDB 2P0N · PDBe 2P0N · UniProt Q9JYL1
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