2X8S

Crystal Structure of the Abn2 D171A mutant in complex with arabinotriose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. ILEMNPKT

Chain	Residue	Details
A	ILE195-THR202

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20883454

Chain	Residue	Details
A	ASP38
B	ASP38

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:20883454

Chain	Residue	Details
A	GLU224
B	GLU224

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP38
A	ASP122
A	ASN168
B	ASP38
B	ASP122
B	ASN168

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:20883454

Chain	Residue	Details
A	SER188
B	SER188

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20883454

Chain	Residue	Details
A	HIS220
B	HIS220

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	HIS318
B	HIS318

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:20883454

Chain	Residue	Details
A	ALA171
B	ALA171

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Important for substrate recognition

Chain	Residue	Details
A	HIS318
B	HIS318

---