Research workbench

Structural characterization of a carbohydrate substrate binding protein from streptococcus pneumoniae

Analyse Structural characterization of a carbohydrate substrate binding protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MLT
Type: protein
Length: 454 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC transporter, substrate-binding protein
UniProt: A0A0H2UMY0
Ligands: ZN
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC transporter, substrate-binding protein	protein	454	42% helix, 15% strand	A0A0H2UMY0

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	818	0.70	0.76	85	empty
2	87	0.41	0.79	20	empty
3	63	0.29	0.73	15	empty
4	53	0.26	0.73	12	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

5MLT · Structural characterization of a carbohydrate substrate binding protein from… · 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 A0A0H2UMY0
Elsewhere: RCSB PDB 5MLT · PDBe 5MLT · UniProt A0A0H2UMY0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.