1NHC

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004650	molecular_function	polygalacturonase activity
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0045490	biological_process	pectin catabolic process
A	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
A	0071555	biological_process	cell wall organization
B	0004650	molecular_function	polygalacturonase activity
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0045490	biological_process	pectin catabolic process
B	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
B	0071555	biological_process	cell wall organization
C	0004650	molecular_function	polygalacturonase activity
C	0005576	cellular_component	extracellular region
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0045490	biological_process	pectin catabolic process
C	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
C	0071555	biological_process	cell wall organization
D	0004650	molecular_function	polygalacturonase activity
D	0005576	cellular_component	extracellular region
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0045490	biological_process	pectin catabolic process
D	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
D	0071555	biological_process	cell wall organization
E	0004650	molecular_function	polygalacturonase activity
E	0005576	cellular_component	extracellular region
E	0005975	biological_process	carbohydrate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0045490	biological_process	pectin catabolic process
E	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
E	0071555	biological_process	cell wall organization
F	0004650	molecular_function	polygalacturonase activity
F	0005576	cellular_component	extracellular region
F	0005975	biological_process	carbohydrate metabolic process
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0045490	biological_process	pectin catabolic process
F	0047911	molecular_function	galacturan 1,4-alpha-galacturonidase activity
F	0071555	biological_process	cell wall organization

Functional Information from PROSITE/UniProt

site_id	PS00502
Number of Residues	14
Details	POLYGALACTURONASE Polygalacturonase active site. GgtCsgGHGLs.IGS

Chain	Residue	Details
A	GLY222-SER235

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	126
Details	Repeat: {"description":"PbH1 1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	180
Details	Repeat: {"description":"PbH1 2"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	126
Details	Repeat: {"description":"PbH1 3"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	126
Details	Repeat: {"description":"PbH1 4"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	132
Details	Repeat: {"description":"PbH1 5"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	270
Details	Repeat: {"description":"PbH1 6"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10052","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	12
Details	Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"source":"PubMed","id":"14623112","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14623112","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP207
A	ASP208
A	ASP186
A	HIS229

---

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

Chain	Residue	Details
B	ASP207
B	ASP208
B	ASP186
B	HIS229

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1czf

Chain	Residue	Details
C	ASP207
C	ASP208
C	ASP186
C	HIS229

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1czf

Chain	Residue	Details
D	ASP207
D	ASP208
D	ASP186
D	HIS229

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1czf

Chain	Residue	Details
E	ASP207
E	ASP208
E	ASP186
E	HIS229

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1czf

Chain	Residue	Details
F	ASP207
F	ASP208
F	ASP186
F	HIS229

---