Research workbench
BLMNBP1 binding protein of an ABC transporter from bifidobacterium animalis subsp. lactis ATCC27673 in complex with mannobiose
Analyse BLMNBP1 binding protein of an ABC transporter from bifidobacterium animalis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I5R
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar ABC transporter substrate-binding protein, BLMNBP1
- Ligands
- BMA, ZN
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sugar ABC transporter substrate-binding protein, BLMNBP1 | protein | 428 | 41% helix, 16% strand | — |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
- ZN · Zinc ion · metal · 14 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.82 | 0.85 | 90 | BMA |
| 2 | 94 | 0.38 | 0.76 | 30 | empty |
Compared structures
- 6I5R · BlMnBP1 binding protein of an ABC transporter from Bifidobacterium animalis subsp. lactis… · 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
- Elsewhere: RCSB PDB 6I5R · PDBe 6I5R
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