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X-ray structure of the galactose mutarotase related enzyme Q5FKD7 from lactobacillus acidophilus at the resolution 1.9A. northeast structural genomics consortium target LAR33.

Analyse X-ray structure of the galactose mutarotase related enzyme Q5FKD7 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DCD
Type: protein
Length: 600 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galactose mutarotase related enzyme
UniProt: Q5FKD7
Pockets: 6 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Galactose mutarotase related enzyme	protein	300	8% helix, 47% strand	Q5FKD7

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	767	0.71	0.78	71	empty
2	155	0.55	0.81	22	empty
3	97	0.52	0.83	23	empty
4	52	0.37	0.80	14	empty
5	65	0.30	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 553 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

3DCD · X-ray structure of the galactose mutarotase related enzyme Q5FKD7 from Lactobacillus… · 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 Q5FKD7
Elsewhere: RCSB PDB 3DCD · PDBe 3DCD · UniProt Q5FKD7

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