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The structure of a putative mannosephosphate isomerase from archaeoglobus fulgidus

Analyse The structure of a putative mannosephosphate isomerase from archaeoglobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZX5
Type: protein
Length: 300 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannosephosphate isomerase, putative
UniProt: O30200
Ligands: LFR
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mannosephosphate isomerase, putative	protein	300	15% helix, 41% strand	O30200

Ligands and binding sites

LFR · beta-L-fructofuranose · ligand · chains A
ACY · Acetic acid · additive · 6 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.57	0.83	24	ACY, GOL
2	159	0.41	0.74	26	EDO

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1ZX5 · The structure of a putative mannosephosphate isomerase from Archaeoglobus fulgidus · 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 O30200
Elsewhere: RCSB PDB 1ZX5 · PDBe 1ZX5 · UniProt O30200

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