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Structural insights into a novel carbohydrate esterase family 7 acetyl xylan esterase from lactococcus lactis

Analyse Structural insights into a novel carbohydrate esterase family 7 acetyl xylan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CUZ
Type: protein
Length: 1,248 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylxylan esterase
EC: 3.1.1.-
UniProt: A9QSE8
Pockets: 15 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Acetylxylan esterase (EC 3.1.1.-)	protein	312	34% helix, 21% strand	A9QSE8

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	803	0.69	0.75	56	empty
2	653	0.66	0.75	79	empty
3	521	0.64	0.76	61	empty
4	442	0.62	0.77	43	empty
5	64	0.59	0.90	17	empty

Interfaces

5 interfaces between chains.

B–D · 1064 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 1053 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 364 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 129 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 17 Å² buried · 0 hydrogen bonds · protein-protein

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 A9QSE8
Elsewhere: RCSB PDB 7CUZ · PDBe 7CUZ · UniProt A9QSE8

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