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Crystal structure of the cellulase CEL9M of C. cellulolyticium in complex with cellobiose

Analyse Crystal structure of the cellulase CEL9M of C. cellulolyticium in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IA7
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase CEL9M
EC: 3.2.1.4
Ligands: BGC, CA, ZN, NI, SO4
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulase CEL9M (EC 3.2.1.4)	protein	431	50% helix, 6% strand	—

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
CA · Calcium ion · metal · chains A
ZN · Zinc ion · metal · chains A
NI · Nickel (II) ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

Pockets

3 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	213	0.50	0.76	26	BGC, SO4, EDO
2	97	0.33	0.73	18	empty
3	59	0.32	0.77	11	empty

Compared structures

1IA7 · Crystal structure of the cellulase CEL9M of C. cellulolyticium in complex with cellobiose · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1IA7 · PDBe 1IA7

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