Research workbench

Endocellulase E1 from acidothermus cellulolyticus mutant Y245G

Analyse Endocellulase E1 from acidothermus cellulolyticus mutant Y245G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VRX
Type: protein
Length: 716 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endocellulase E1 from a. cellulolyticus
EC: 3.2.1.4
UniProt: P54583
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endocellulase E1 from a. cellulolyticus (EC 3.2.1.4)	protein	358	28% helix, 18% strand	P54583

Pockets

7 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	869	0.77	0.80	60	empty
2	246	0.52	0.76	31	empty
3	185	0.45	0.75	28	empty
4	85	0.37	0.76	23	empty
5	83	0.35	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 809 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1VRX · Endocellulase e1 from acidothermus cellulolyticus mutant y245g · the same entry in another collection · chain A against A, TM-score 1.00
P54583 · AlphaFold monomer V2.0 prediction for endoglucanase E1 (P54583) · 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 P54583
Elsewhere: RCSB PDB 1VRX · PDBe 1VRX · UniProt P54583

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