MolNFT v1 · #8582 · protein

Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography

1H52: “Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray…”. X-ray diffraction, 1 ligand (POP), 1 pocket (best druggability 0.31). MolNFT v1 #8582 on GenesisL1: 3D structure, binding…

PDB: 1H52
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiogenin
UniProt: P03950
Ligands: POP
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiogenin	protein	122	28% helix, 34% strand	P03950

Ligands and binding sites

POP · Pyrophosphate 2- · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.31	0.76	15	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1H52 · Binding of Phosphate and Pyrophosphate ions at the active site of human Angiogenin as… · the same entry in another collection · chain A against A, TM-score 1.00
P03950 · AlphaFold monomer V2.0 prediction for angiogenin (P03950) · 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 P03950
Elsewhere: RCSB PDB 1H52 · PDBe 1H52 · UniProt P03950

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