Research workbench

Crystal structure of catalytic domain of E.COLI rluf

Analyse Crystal structure of catalytic domain of E.COLI rluf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GML
Type: protein
Length: 350 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosomal large subunit pseudouridine synthase F
EC: 5.4.99.-
UniProt: P32684
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribosomal large subunit pseudouridine synthase F (EC 5.4.99.-)	protein	175	23% helix, 31% strand	P32684

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.59	0.86	26	empty
2	166	0.57	0.82	25	empty
3	175	0.41	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 188 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2GML · Crystal Structure of Catalytic Domain of E.coli RluF · the same entry in another collection · chain A against A, TM-score 1.00
P32684 · AlphaFold monomer V2.0 prediction for dual-specificity RNA pseudouridine synthase rluf… · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P32684
Elsewhere: RCSB PDB 2GML · PDBe 2GML · UniProt P32684

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