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Enzyme-ligand complex of P. aeruginosa PMM/PGM

Analyse Enzyme-ligand complex of P. aeruginosa PMM/PGM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P5G
Type: protein
Length: 455 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphomannomutase
EC: 5.4.2.8
UniProt: P26276
Ligands: G6P, ZN
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Phosphomannomutase (EC 5.4.2.8)	protein	455	38% helix, 24% strand	P26276

Ligands and binding sites

G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains X
ZN · Zinc ion · metal · chains X

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

Pockets

3 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	442	0.69	0.81	59	G6P
2	119	0.49	0.80	18	empty
3	60	0.33	0.77	17	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1P5G · Enzyme-ligand complex of P. aeruginosa PMM/PGM · the same entry in another collection · chain X against X, TM-score 1.00
P26276 · AlphaFold monomer V2.0 prediction for PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (P26276) · a predicted model of the same protein · chain X 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 P26276
Elsewhere: RCSB PDB 1P5G · PDBe 1P5G · UniProt P26276

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