MolNFT v1 · #119765 · protein

S.PNEUMONIAE ABC-transporter substrate binding protein fusa ef-hand mutant in complex with fructo-nystose

5G62 · ABC transporter, substrate-binding protein: “S.PNEUMONIAE ABC-transporter substrate binding protein fusa ef-hand mutant in complex with fructo-nystose”. X-ray diffraction, 4 ligands (ZEE, UEA, FRU), 16 pockets (best druggability…

PDB: 5G62
Type: protein
Length: 982 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC transporter, substrate-binding protein
UniProt: A0A0H2URD6
Ligands: ZEE, UEA, FRU, CA
Pockets: 16 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ABC transporter, substrate-binding protein	protein	491	45% helix, 14% strand	A0A0H2URD6

Ligands and binding sites

ZEE · beta-L-talopyranose · ligand · 2 copies · chains A, B
UEA · beta-D-sorbofuranose · ligand · 2 copies
FRU · beta-D-fructofuranose · sugar · 6 copies · chains A, B
CA · Calcium ion · metal · 3 copies · chains A, B

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

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	334	0.69	0.83	45	UEA, FRU
2	310	0.67	0.82	44	FRU
3	199	0.66	0.85	24	empty
4	279	0.65	0.81	35	empty
5	314	0.64	0.80	36	empty

Interfaces

1 interface between chains.

A–B · 1540 Å² buried · 26 hydrogen bonds · protein-protein

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 A0A0H2URD6
Elsewhere: RCSB PDB 5G62 · PDBe 5G62 · UniProt A0A0H2URD6

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