1FHL

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015926	molecular_function	glucosidase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
A	0045490	biological_process	pectin catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	GLU136

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	GLU246

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN112

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12484750

Chain	Residue	Details
A	GLU136
A	GLU246
A	ARG45

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 658

Chain	Residue	Details
A	ARG45	electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity, modifies pKa
A	GLU136	activator, increase nucleophilicity, proton acceptor, proton donor
A	GLU246	covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile

---