MolNFT v1 · #20489 · protein

The complex between ribonuclease T1 and 3'-guanylic acid suggests geometry of enzymatic reaction path. an X-ray study

1RGC: “The complex between ribonuclease T1 and 3'-guanylic acid suggests geometry of enzymatic reaction path. an…”. X-ray diffraction, 2 ligands (3GP, CA). MolNFT v1 #20489 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1RGC
Type: protein
Length: 208 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease T1
EC: 3.1.27.3
UniProt: P00651
Ligands: 3GP, CA

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease T1 (EC 3.1.27.3)	protein	104	16% helix, 29% strand	P00651

Ligands and binding sites

3GP · Guanosine-3'-monophosphate · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 142 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1RGC · The complex between ribonuclease T1 and 3'-guanylic acid suggests geometry of enzymatic… · the same entry in another collection · chain A against A, TM-score 1.00
P00651 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease T1 (P00651) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00651
Elsewhere: RCSB PDB 1RGC · PDBe 1RGC · UniProt P00651

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.