MolNFT v1 · #25589 · protein

Crystal structure of the bifunctional protein pria

1VZW · Phosphoribosyl isomerase a: “Crystal structure of the bifunctional protein pria”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.64). MolNFT v1 #25589 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VZW
Type: protein
Length: 224 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoribosyl isomerase a
EC: 5.3.1.15, 5.3.1.24
UniProt: P16250
Ligands: SO4
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoribosyl isomerase a (EC 5.3.1.15, 5.3.1.24)	protein	224	42% helix, 24% strand	P16250

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	336	0.64	0.80	36	SO4
2	62	0.59	0.90	16	GOL

Compared structures

1VZW · Crystal structure of the bifunctional protein Pria · the same entry in another collection · chain A against A, TM-score 1.00
P16250 · AlphaFold monomer V2.0 prediction for phosphoribosyl isomerase a (P16250) · 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 P16250
Elsewhere: RCSB PDB 1VZW · PDBe 1VZW · UniProt P16250

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