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Crystal structure of the N-terminal carbohydrate binding module family 48 and ferulic acid esterase from the multi-enzyme CE1-GH62-GH10

Analyse Crystal structure of the N-terminal carbohydrate binding module family 48 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RZN
Type: protein
Length: 678 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferulic acid esterase
EC: 3.1.1.73
Pockets: 10 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferulic acid esterase (EC 3.1.1.73)	protein	338	28% helix, 28% strand	—
B	Ferulic acid esterase (EC 3.1.1.73)	protein	340	27% helix, 28% strand	—

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.85	0.93	54	empty
2	255	0.62	0.81	23	empty
3	82	0.40	0.78	19	empty
4	78	0.40	0.78	19	empty
5	113	0.38	0.74	25	empty

Interfaces

1 interface between chains.

A–B · 1735 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6RZN · Crystal structure of the N-terminal carbohydrate binding module family 48 and ferulic… · 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
Elsewhere: RCSB PDB 6RZN · PDBe 6RZN

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