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Beta-1,4-D-endoglucanase CEL45A from blue mussel mytilus edulis at 1.2A

Analyse Beta-1,4-D-endoglucanase CEL45A from blue mussel mytilus edulis at 1.2A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WC2
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase
EC: 3.2.1.4
UniProt: P82186

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase (EC 3.2.1.4)	protein	180	13% helix, 29% strand	P82186

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1WC2 · Beta-1,4-D-endoglucanase Cel45A from blue mussel Mytilus edulis at 1.2A · the same entry in another collection · chain A against A, TM-score 1.00
P82186 · AlphaFold monomer V2.0 prediction for endoglucanase (P82186) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P82186
Elsewhere: RCSB PDB 1WC2 · PDBe 1WC2 · UniProt P82186

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