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The humicola grisea CEL12A enzyme structure at 1.2 a resolution

Analyse The humicola grisea CEL12A enzyme structure at 1.2 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OLR
Type: protein
Length: 224 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-glucanase
EC: 3.2.1.4
UniProt: Q8NJY3
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-glucanase (EC 3.2.1.4)	protein	224	9% helix, 54% strand	Q8NJY3

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	173	0.52	0.78	27	empty

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).

Compared structures

1OLR · The Humicola grisea Cel12A Enzyme Structure at 1.2 A Resolution · 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 Q8NJY3
Elsewhere: RCSB PDB 1OLR · PDBe 1OLR · UniProt Q8NJY3

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