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Crystal structure of the catalytic domain of a thermophilic endocellulase

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

PDB: 1TML
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-D-glucanase
EC: 3.2.1.4
UniProt: P26222
Ligands: SO4
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-D-glucanase (EC 3.2.1.4)	protein	286	39% helix, 13% strand	P26222

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.50	0.75	33	empty
2	50	0.43	0.84	17	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1TML · Crystal structure of the catalytic domain of a thermophilic endocellulase · the same entry in another collection · chain A against A, TM-score 1.00
P26222 · AlphaFold monomer V2.0 prediction for endoglucanase E-2 (P26222) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P26222
Elsewhere: RCSB PDB 1TML · PDBe 1TML · UniProt P26222

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