MolNFT v1 · #35209 · protein

Thermodynamic and structural analysis of thermolabile RNase hi from shewanella oneidensis mr-1

2E4L · Ribonuclease hi: “Thermodynamic and structural analysis of thermolabile RNase hi from shewanella oneidensis mr-1”. X-ray diffraction, 1 pocket (best druggability 0.35). MolNFT v1 #35209 on GenesisL1: 3D structure, binding sites and…

PDB: 2E4L
Type: protein
Length: 155 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease hi
EC: 3.1.26.4
UniProt: Q8EE30
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease hi (EC 3.1.26.4)	protein	155	36% helix, 30% strand	Q8EE30

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.35	0.76	13	empty

Compared structures

2E4L · Thermodynamic and Structural Analysis of Thermolabile RNase HI from Shewanella oneidensis… · the same entry in another collection · chain A against A, TM-score 1.00
Q8EE30 · AlphaFold monomer V2.0 prediction for ribonuclease hi (Q8EE30) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8EE30
Elsewhere: RCSB PDB 2E4L · PDBe 2E4L · UniProt Q8EE30

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