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X-ray structure of human phosphomannomutase 2 (PMM2)

Analyse X-ray structure of human phosphomannomutase 2 (PMM2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AMY
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphomannomutase 2
EC: 5.4.2.8
UniProt: O15305
Ligands: GLY
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphomannomutase 2 (EC 5.4.2.8)	protein	240	40% helix, 23% strand	O15305

Ligands and binding sites

GLY · Glycine · ligand · 3 copies · 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

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	195	0.47	0.75	21	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2AMY · X-Ray Structure of Human Phosphomannomutase 2 (PMM2) · the same entry in another collection · chain A against A, TM-score 1.00
O15305 · AlphaFold monomer V2.0 prediction for phosphomannomutase 2 (O15305) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O15305
Elsewhere: RCSB PDB 2AMY · PDBe 2AMY · UniProt O15305

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