6CEL

CBH1 (E212Q) CELLOPENTAOSE COMPLEX

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

Functional Information from PDB Data

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

Chain	Residue
A	GLN212
A	ASP214
A	GLU217
A	HIS228

---

site_id	COB
Number of Residues	3
Details	COBALT-BINDING SITE ON CRYSTALLOGRAPHIC DYAD. THE METAL ION IS BOUND BY GLU 295 AND GLU 325 FROM TWO CRYSTALLOGRAPHICALLY RELATED MOLECULES.

Chain	Residue
A	GLU295
A	GLU325
A	CO1000

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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	MCSA1
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
A	TRP216	covalent catalysis
A	ALA218	modifies pKa
A	ILE221	proton shuttle (general acid/base)
A	THR232	modifies pKa

---