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Crystal structure of a sugar phosphate ISOMERASE/EPIMERASE (BDI_1903) from parabacteroides distasonis atcc 8503 at 1.85 a resolution

Analyse Crystal structure of a sugar phosphate ISOMERASE/EPIMERASE (BDI_1903) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P6L
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sugar phosphate ISOMERASE/EPIMERASE
UniProt: A6LD74
Ligands: PO4
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sugar phosphate ISOMERASE/EPIMERASE	protein	262	41% helix, 20% strand	A6LD74

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
CIT · Citric acid · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.38	0.81	14	empty
2	57	0.27	0.74	16	CIT

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3P6L · Crystal structure of a Sugar phosphate isomerase/epimerase (BDI_1903) 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 A6LD74
Elsewhere: RCSB PDB 3P6L · PDBe 3P6L · UniProt A6LD74

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