Research workbench

E. COLI RNase 1 (in vivo folded)

Analyse E. COLI RNase 1 (in vivo folded) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PQX
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease I
EC: 3.1.27.6
UniProt: P21338
Ligands: CA
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease I (EC 3.1.27.6)	protein	245	43% helix, 16% strand	P21338

Ligands and binding sites

CA · Calcium ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	384	0.63	0.78	46	empty
2	54	0.30	0.76	14	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2PQX · E. coli RNase 1 (in vivo folded) · the same entry in another collection · chain A against A, TM-score 1.00
P21338 · AlphaFold monomer V2.0 prediction for ribonuclease I (P21338) · 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 P21338
Elsewhere: RCSB PDB 2PQX · PDBe 2PQX · UniProt P21338

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