MolNFT v1 · #139046 · protein

Crystal structure of D-mannose isomerase

5X32 · N-acylglucosamine 2-epimerase: “Crystal structure of D-mannose isomerase”. X-ray diffraction, 1 ligand (PO4), 6 pockets (best druggability 0.76). MolNFT v1 #139046 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5X32
Type: protein
Length: 771 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acylglucosamine 2-epimerase
UniProt: F2JVT6
Ligands: PO4
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acylglucosamine 2-epimerase	protein	380	53% helix, 12% strand	F2JVT6
B	N-acylglucosamine 2-epimerase	protein	391	51% helix, 13% strand	F2JVT6

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	903	0.76	0.79	75	PO4
2	559	0.74	0.81	42	PO4
3	165	0.68	0.88	25	empty
4	129	0.67	0.89	25	empty
5	73	0.37	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 545 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5X32 · Crystal structure of D-mannose isomerase · 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 F2JVT6
Elsewhere: RCSB PDB 5X32 · PDBe 5X32 · UniProt F2JVT6

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