Research workbench

Arh-I, an ANGIOGENIN/RNASE a chimera

Analyse Arh-I, an ANGIOGENIN/RNASE a chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GV7
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiogenin
EC: 3.1.27.5
UniProt: P03950, P00656

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiogenin (EC 3.1.27.5)	protein	123	27% helix, 32% strand	P03950, P00656

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.

Modifications

Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).

Compared structures

1GV7 · ARH-I, an angiogenin/RNase A chimera · 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 0.94

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
Every structure of UniProt P00656
Elsewhere: RCSB PDB 1GV7 · PDBe 1GV7 · UniProt P03950 · UniProt P00656

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