Research workbench

Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney

Analyse Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FP3
Type: protein
Length: 804 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acyl-D-glucosamine 2-epimerase
EC: 5.1.3.8
UniProt: P17560
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	N-acyl-D-glucosamine 2-epimerase (EC 5.1.3.8)	protein	402	58% helix, 10% strand	P17560

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	368	0.78	0.88	36	empty
2	611	0.72	0.80	55	empty
3	97	0.72	0.94	16	empty
4	520	0.71	0.80	47	empty
5	591	0.69	0.78	56	empty

Interfaces

1 interface between chains.

A–B · 1162 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

1FP3 · Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney · the same entry in another collection · chain A against A, TM-score 1.00
P17560 · AlphaFold monomer V2.0 prediction for N-acylglucosamine 2-epimerase (P17560) · a predicted model of the same protein · 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 P17560
Elsewhere: RCSB PDB 1FP3 · PDBe 1FP3 · UniProt P17560

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