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Structure of human alpha-phosphomannomutase 1 in complex with inosine monophosphate

Analyse Structure of human alpha-phosphomannomutase 1 in complex with inosine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CFV
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphomannomutase 1
EC: 5.4.2.8
UniProt: Q92871
Ligands: IMP, MG
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphomannomutase 1 (EC 5.4.2.8)	protein	245	39% helix, 19% strand	Q92871

Ligands and binding sites

IMP · Inosinic acid · ligand · chains A
MG · Magnesium ion · metal · 2 copies · 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	372	0.60	0.77	44	MG, IMP
2	50	0.29	0.76	14	empty

Compared structures

6CFV · Structure of Human alpha-Phosphomannomutase 1 in complex with Inosine Monophosphate · the same entry in another collection · chain A against A, TM-score 1.00
Q92871 · AlphaFold monomer V2.0 prediction for phosphomannomutase 1 (Q92871) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q92871
Elsewhere: RCSB PDB 6CFV · PDBe 6CFV · UniProt Q92871

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