MolNFT v1 · #20493 · protein

Hydrolase, guanyloribonuclease

1RGG: “Hydrolase, guanyloribonuclease”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.49). MolNFT v1 #20493 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1RGG
Type: protein
Length: 192 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease
EC: 3.1.27.3
UniProt: P05798
Ligands: SO4
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease (EC 3.1.27.3)	protein	96	16% helix, 21% strand	P05798

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.49	0.80	26	empty
2	112	0.43	0.77	21	empty

Interfaces

1 interface between chains.

A–B · 241 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1RGG · Hydrolase, guanyloribonuclease · the same entry in another collection · chain A against A, TM-score 1.00
P05798 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease sa (P05798) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P05798
Elsewhere: RCSB PDB 1RGG · PDBe 1RGG · UniProt P05798

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