MolNFT v1 · #32999 · protein

The structure of a family 4 acetyl xylan esterase from clostridium thermocellum in complex with a magnesium ion.

2C71 · Glycoside hydrolase, family 11\:CLOSTRIDIUM cellulosome…: “The structure of a family 4 acetyl xylan esterase from clostridium thermocellum in complex with a magnesium…”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability…

PDB: 2C71
Type: protein
Length: 205 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase, family 11\:CLOSTRIDIUM cellulosome enzyme, dockerin type…
EC: 3.1.1.72
UniProt: Q4CFF1
Ligands: MG
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase, family 11\:CLOSTRIDIUM cellulosome enzyme, dockerin type I\:POLYSACCHARIDE (EC 3.1.1.72)	protein	205	44% helix, 15% strand	Q4CFF1

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.31	0.77	15	MG

Compared structures

2C71 · The structure of a family 4 acetyl xylan esterase from Clostridium thermocellum in… · 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 Q4CFF1
Elsewhere: RCSB PDB 2C71 · PDBe 2C71 · UniProt Q4CFF1

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