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Crystal structure of mannose 6-phosphate isomerase (holo; zinc bound)

Analyse Crystal structure of mannose 6-phosphate isomerase (holo; zinc bound) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H1M
Type: protein
Length: 392 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannose-6-phosphate isomerase
EC: 5.3.1.8
UniProt: P25081
Ligands: ZN
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mannose-6-phosphate isomerase (EC 5.3.1.8)	protein	392	28% helix, 30% strand	P25081

Ligands and binding sites

ZN · Zinc ion · metal · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A

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	504	0.68	0.78	41	EDO
2	83	0.38	0.77	16	empty
3	74	0.36	0.77	18	empty

Compared structures

3H1M · Crystal structure of mannose 6-phosphate isomerase (holo; zinc bound) · the same entry in another collection · chain A against A, TM-score 1.00
P25081 · AlphaFold monomer V2.0 prediction for mannose-6-phosphate isomerase (P25081) · 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 P25081
Elsewhere: RCSB PDB 3H1M · PDBe 3H1M · UniProt P25081

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