Research workbench

Endoglucanase CEL12A from rhodothermus marinus

Analyse Endoglucanase CEL12A from rhodothermus marinus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H0B
Type: protein
Length: 452 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase
EC: 3.2.1.4
UniProt: O33897
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellulase (EC 3.2.1.4)	protein	226	7% helix, 53% strand	O33897

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B

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

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	412	0.65	0.78	50	EPE
2	275	0.59	0.78	40	EPE
3	124	0.42	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 489 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1H0B · Endoglucanase cel12A from Rhodothermus marinus · 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 O33897
Elsewhere: RCSB PDB 1H0B · PDBe 1H0B · UniProt O33897

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