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Crystal structure of the cellulase CEL9M of C. cellulolyticum

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

PDB: 1IA6
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase CEL9M
EC: 3.2.1.4
UniProt: Q9EYQ2
Ligands: CA, ZN, NI, SO4
Pockets: 4 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulase CEL9M (EC 3.2.1.4)	protein	423	50% helix, 5% strand	Q9EYQ2

Ligands and binding sites

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

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	172	0.48	0.76	25	SO4
2	58	0.42	0.82	15	empty
3	88	0.37	0.76	21	empty
4	60	0.30	0.75	19	empty

Compared structures

1IA6 · Crystal structure of the cellulase CEL9M of C. cellulolyticum · 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 Q9EYQ2
Elsewhere: RCSB PDB 1IA6 · PDBe 1IA6 · UniProt Q9EYQ2

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