2CEL

ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE

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 PDB Data

site_id	CAA
Number of Residues	4
Details	CALCIUM-BINDING SITE ON NON-CRYSTALLOGRAPHIC DYAD. NOTE THAT THE CALCIUM ION IS BOUND BY GLU 295 AND GLU 325 FROM TWO NCS-RELATED MOLECULES, AND ONE WATER MOLECULE POSITIONED EXACTLY ON THE NCS-AXIS.

Chain	Residue
A	CA1000
A	HOH1001
A	GLU295
A	GLU325

---

site_id	CAB
Number of Residues	4
Details	CALCIUM-BINDING SITE ON NON-CRYSTALLOGRAPHIC DYAD. NOTE THAT THE CALCIUM ION IS BOUND BY GLU 295 AND GLU 325 FROM TWO NCS-RELATED MOLECULES, AND ONE WATER MOLECULE POSITIONED EXACTLY ON THE NCS-AXIS.

Chain	Residue
B	CA1000
B	HOH1001
B	GLU295
B	GLU325

---

site_id	CTA
Number of Residues	4
Details	CATALYTIC SITE INCLUDING THE E212Q MUTATION.

Chain	Residue
A	GLN212
A	ASP214
A	GLU217
A	HIS228

---

site_id	CTB
Number of Residues	4
Details	CATALYTIC SITE INCLUDING THE E212Q MUTATION.

Chain	Residue
B	ASP214
B	GLU217
B	HIS228
B	GLN212

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495

Chain	Residue	Details
A	GLN212
B	GLN212

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495

Chain	Residue	Details
A	GLU217
B	GLU217

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Not glycosylated => ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN64
B	ASN64

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|DOI:10.1016/0014-5793(80)81006-4, ECO:0000269|DOI:10.1038/nbt1083-687, ECO:0007744|PDB:1EGN, ECO:0007744|PDB:1Q2B, ECO:0007744|PDB:1Q2E

Chain	Residue	Details
A	PCA1
B	PCA1

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN45
B	ASN45

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:24341799, ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911, ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN270
B	ASN270

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:24341799, ECO:0000269|PubMed:9466911, ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN384
B	ASN384

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1cel

Chain	Residue	Details
A	GLN212
A	HIS228
A	ASP214
A	GLU217

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1cel

Chain	Residue	Details
B	GLN212
B	HIS228
B	ASP214
B	GLU217

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
A	GLN212	covalent catalysis
A	ASP214	modifies pKa
A	GLU217	proton shuttle (general acid/base)
A	HIS228	modifies pKa

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
B	GLN212	covalent catalysis
B	ASP214	modifies pKa
B	GLU217	proton shuttle (general acid/base)
B	HIS228	modifies pKa

---