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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: 6I5W
Type: protein
Length: 427 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute binding protein BLMNBP1, BLAC_00780 in complex with mannopentaose
Ligands: BMA, ZN
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Solute binding protein BLMNBP1, BLAC_00780 in complex with mannopentaose	protein	427	40% helix, 16% strand	—

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 5 copies · chains A
ZN · Zinc ion · metal · 17 copies · chains A
ACT · Acetate ion · additive · 7 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	875	0.82	0.84	75	BMA

Compared structures

6I5W · 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 6I5W · PDBe 6I5W

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