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Crystal structure of human angiogenin variant Q117G

Analyse Crystal structure of human angiogenin variant Q117G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K59
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiogenin
EC: 3.1.27.-
UniProt: P03950
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiogenin (EC 3.1.27.-)	protein	123	26% helix, 36% strand	P03950

Ligands and binding sites

CIT · Citric acid · additive · 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	52	0.26	0.74	17	empty

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, cyclization).

Compared structures

1K59 · Crystal Structure of Human Angiogenin Variant Q117G · 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 1K59 · PDBe 1K59 · UniProt P03950

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