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Crystal structure of a glycoside hydrolase family 44 endoglucanase produced by clostridium acetobutylium atcc 824

Analyse Crystal structure of a glycoside hydrolase family 44 endoglucanase produced by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IK2
Type: protein
Length: 512 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase a
UniProt: Q977Y3
Ligands: CA, CL, SO4
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase a	protein	512	31% helix, 26% strand	Q977Y3

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 9 copies · chains A
ACT · Acetate ion · additive · 4 copies · 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	235	0.53	0.76	42	GOL
2	69	0.36	0.77	14	empty

Compared structures

3IK2 · Crystal Structure of a Glycoside Hydrolase Family 44 Endoglucanase produced by… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q977Y3
Elsewhere: RCSB PDB 3IK2 · PDBe 3IK2 · UniProt Q977Y3

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