3AQU

Crystal structure of a class V chitinase from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004568	molecular_function	chitinase activity
A	0005576	cellular_component	extracellular region
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	0009505	cellular_component	plant-type cell wall
A	0009651	biological_process	response to salt stress
A	0009737	biological_process	response to abscisic acid
A	0009753	biological_process	response to jasmonic acid
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0035885	molecular_function	exochitinase activity
A	0099503	cellular_component	secretory vesicle
B	0000272	biological_process	polysaccharide catabolic process
B	0004568	molecular_function	chitinase activity
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0006032	biological_process	chitin catabolic process
B	0008061	molecular_function	chitin binding
B	0008843	molecular_function	endochitinase activity
B	0009505	cellular_component	plant-type cell wall
B	0009651	biological_process	response to salt stress
B	0009737	biological_process	response to abscisic acid
B	0009753	biological_process	response to jasmonic acid
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0035885	molecular_function	exochitinase activity
B	0099503	cellular_component	secretory vesicle
C	0000272	biological_process	polysaccharide catabolic process
C	0004568	molecular_function	chitinase activity
C	0005576	cellular_component	extracellular region
C	0005975	biological_process	carbohydrate metabolic process
C	0006032	biological_process	chitin catabolic process
C	0008061	molecular_function	chitin binding
C	0008843	molecular_function	endochitinase activity
C	0009505	cellular_component	plant-type cell wall
C	0009651	biological_process	response to salt stress
C	0009737	biological_process	response to abscisic acid
C	0009753	biological_process	response to jasmonic acid
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0035885	molecular_function	exochitinase activity
C	0099503	cellular_component	secretory vesicle
D	0000272	biological_process	polysaccharide catabolic process
D	0004568	molecular_function	chitinase activity
D	0005576	cellular_component	extracellular region
D	0005975	biological_process	carbohydrate metabolic process
D	0006032	biological_process	chitin catabolic process
D	0008061	molecular_function	chitin binding
D	0008843	molecular_function	endochitinase activity
D	0009505	cellular_component	plant-type cell wall
D	0009651	biological_process	response to salt stress
D	0009737	biological_process	response to abscisic acid
D	0009753	biological_process	response to jasmonic acid
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0035885	molecular_function	exochitinase activity
D	0099503	cellular_component	secretory vesicle

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE FLC A 356

Chain	Residue
A	HIS247
D	VAL281
D	TYR290
D	TYR292
A	SER248
A	VAL281
A	TYR290
A	TYR292
A	HOH367
A	HOH418
D	HIS247
D	SER248

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FLC A 357

Chain	Residue
A	THR54
A	THR58
A	ARG61
A	HOH439
A	HOH574
B	SER87
B	PRO89
B	ARG92
B	HOH437

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FLC B 356

Chain	Residue
B	HIS247
B	SER248
B	VAL281
B	TYR290
B	TYR292
B	HOH512
C	HIS247
C	SER248
C	TYR290
C	TYR292

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1368
Details	Domain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21390509","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21390509","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21390509","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---