Research workbench

Mutant human ribonuclease 1 (R31L, R32L)

Analyse Mutant human ribonuclease 1 (R31L, R32L) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E0J
Type: protein
Length: 256 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease
EC: 3.1.27.5
UniProt: P07998
Pockets: 4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease (EC 3.1.27.5)	protein	128	20% helix, 38% strand	P07998

Pockets

4 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	63	0.50	0.86	22	empty
2	56	0.37	0.80	18	empty
3	71	0.36	0.77	16	empty
4	73	0.31	0.74	26	empty

Interfaces

1 interface between chains.

A–B · 728 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

2E0J · Mutant Human Ribonuclease 1 (R31L, R32L) · the same entry in another collection · chain A against A, TM-score 1.00
P07998 · AlphaFold monomer V2.0 prediction for ribonuclease pancreatic (P07998) · 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 P07998
Elsewhere: RCSB PDB 2E0J · PDBe 2E0J · UniProt P07998

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