1NH6

Structure of S. marcescens chitinase A, E315L, complex with hexasaccharide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004568	molecular_function	chitinase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0006032	biological_process	chitin catabolic process
A	0008061	molecular_function	chitin binding
A	0008843	molecular_function	endochitinase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	401
Details	Domain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ctn

Chain	Residue	Details
A	ASP313
A	LEU315
A	TYR390

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ctn

Chain	Residue	Details
A	ASP313
A	LEU315

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ctn

Chain	Residue	Details
A	ASP311
A	LEU315

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 478

Chain	Residue	Details
A	ASP311	electrostatic stabiliser
A	ASP313	steric role
A	LEU315	proton shuttle (general acid/base)
A	TYR390	electrostatic destabiliser

---