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Crystal structure of a putative two-domain sugar hydrolase (BACCAC_02064) from bacteroides caccae atcc 43185 at 1.80 a resolution

Analyse Crystal structure of a putative two-domain sugar hydrolase (BACCAC_02064) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QHX
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A5ZGP5
Ligands: SO4, CL
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	400	10% helix, 55% strand	A5ZGP5

Ligands and binding sites

SO4 · Sulfate ion · ion · 9 copies · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 7 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	93	0.36	0.74	22	SO4

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4QHX · Crystal structure of a putative two-domain sugar hydrolase (BACCAC_02064) 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 A5ZGP5
Elsewhere: RCSB PDB 4QHX · PDBe 4QHX · UniProt A5ZGP5

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