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Structure of mpt-4, a mannose phosphorylase from leishmania mexicana, in complex with phosphate ion

Analyse Structure of mpt-4, a mannose phosphorylase from leishmania mexicana, in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q50
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mpt-4
UniProt: E9ANE0
Ligands: NA, PO4
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mpt-4	protein	318	9% helix, 53% strand	E9ANE0

Ligands and binding sites

NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.59	0.82	27	empty
2	125	0.51	0.81	29	PO4, NA
3	52	0.42	0.83	18	empty
4	81	0.38	0.77	14	empty

Compared structures

6Q50 · Structure of MPT-4, a mannose phosphorylase from Leishmania mexicana, in complex with… · 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 E9ANE0
Elsewhere: RCSB PDB 6Q50 · PDBe 6Q50 · UniProt E9ANE0

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