MolNFT v1 · #18687 · protein

Crystal structure of human pnp complexed with acyclovir

1PWY · Purine nucleoside phosphorylase: “Crystal structure of human pnp complexed with acyclovir”. X-ray diffraction, 2 ligands (AC2, SO4), 1 pocket (best druggability 0.63). MolNFT v1 #18687 on GenesisL1: 3D structure, binding sites and…

PDB: 1PWY
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Purine nucleoside phosphorylase
EC: 2.4.2.1
UniProt: P00491
Ligands: AC2, SO4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Purine nucleoside phosphorylase (EC 2.4.2.1)	protein	288	31% helix, 19% strand	P00491

Ligands and binding sites

AC2 · 9-hyroxyethoxymethylguanine · ligand · chains E
SO4 · Sulfate ion · ion · 3 copies · chains E

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	251	0.63	0.81	39	SO4, AC2

Compared structures

1PWY · Crystal structure of human pnp complexed with acyclovir · the same entry in another collection · chain E against E, TM-score 1.00
P00491 · AlphaFold monomer V2.0 prediction for purine nucleoside phosphorylase (P00491) · a predicted model of the same protein · chain E against A, TM-score 0.95

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 P00491
Elsewhere: RCSB PDB 1PWY · PDBe 1PWY · UniProt P00491

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