Research workbench

Crystal structure of RRP1 from chaetomium thermophilum in space group C2

Analyse Crystal structure of RRP1 from chaetomium thermophilum in space group C2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EMF
Type: protein
Length: 461 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: G0S4M2
UniProt: G0S4M2
Ligands: PRO
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	G0S4M2	protein	228	70% helix, 4% strand	G0S4M2
B	G0S4M2	protein	233	70% helix, 3% strand	G0S4M2

Ligands and binding sites

PRO · Proline · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1182	0.75	0.78	83	PRO

Interfaces

1 interface between chains.

A–B · 637 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6EMF · Crystal structure of Rrp1 from Chaetomium thermophilum in space group C2 · the same entry in another collection · 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 G0S4M2
Elsewhere: RCSB PDB 6EMF · PDBe 6EMF · UniProt G0S4M2

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