MolNFT v1 · #52923 · protein

Structure of beta-phosphoglucomutase inhibited with beryllium trifluoride, in an open conformation.

2WFA: “Structure of beta-phosphoglucomutase inhibited with beryllium trifluoride, in an open conformation.”. X-ray diffraction, 2 ligands (BEF, MG), 1 pocket (best druggability 0.65). MolNFT v1 #52923 on GenesisL1: 3D structure, binding…

PDB: 2WFA
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-phosphoglucomutase
EC: 5.4.2.6
UniProt: P71447
Ligands: BEF, MG
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-phosphoglucomutase (EC 5.4.2.6)	protein	221	53% helix, 11% strand	P71447

Ligands and binding sites

BEF · Beryllium trifluoride ion · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	430	0.65	0.78	43	MG, BEF

Compared structures

2WFA · Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open… · the same entry in another collection · chain A against A, TM-score 1.00
P71447 · AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (P71447) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P71447
Elsewhere: RCSB PDB 2WFA · PDBe 2WFA · UniProt P71447

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