Research workbench
Glnh bound to asn, mycobacterium tuberculosis
Analyse Glnh bound to asn, mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H20
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable glutamine-binding lipoprotein glnh (glnbp)
- UniProt
- P96257
- Ligands
- ASN
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable glutamine-binding lipoprotein glnh (glnbp) | protein | 287 | 35% helix, 22% strand | P96257 |
Ligands and binding sites
- ASN · Asparagine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.51 | 0.75 | 35 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6H20 · GlnH bound to Asn, Mycobacterium tuberculosis · 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 P96257
- Elsewhere: RCSB PDB 6H20 · PDBe 6H20 · UniProt P96257
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