1T6G

Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0045493	biological_process	xylan catabolic process
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0045493	biological_process	xylan catabolic process
C	0000272	biological_process	polysaccharide catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
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	0031176	molecular_function	endo-1,4-beta-xylanase activity
C	0045493	biological_process	xylan catabolic process
D	0000272	biological_process	polysaccharide catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
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	0031176	molecular_function	endo-1,4-beta-xylanase activity
D	0045493	biological_process	xylan catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL C 2158

Chain	Residue
A	VAL273
C	GLY105
C	HOH1323
A	GLY280
A	VAL281
A	CYS282
A	HOH1090
A	HOH1620
C	TYR102
C	SER103
C	ASP104

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL D 2159

Chain	Residue
B	VAL273
B	GLY280
B	VAL281
B	CYS282
B	HOH1161
B	HOH1756
D	TYR102
D	SER103
D	ASP104
D	GLY105
D	HOH1386

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 2160

Chain	Residue
C	GLY15
C	ASP16
C	TYR29
C	TRP30
C	GLU31
C	ASP32
C	HOH1290
C	HOH1646
C	HOH1883

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 2161

Chain	Residue
D	GLY15
D	ASP16
D	TYR29
D	TRP30
D	GLU31
D	ASP32
D	HOH1281
D	HOH1687
D	HOH1726

---

Functional Information from PROSITE/UniProt

site_id	PS00776
Number of Residues	11
Details	GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PQaEYYIVEdY

Chain	Residue	Details
C	PRO76-TYR86

---

site_id	PS00777
Number of Residues	12
Details	GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MavEAWSGAGsA

Chain	Residue	Details
C	MET167-ALA178

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER235

---

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

Chain	Residue	Details
B	SER235

---

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

Chain	Residue	Details
C	GLU170
C	GLU79

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bvv

Chain	Residue	Details
D	GLU170
D	GLU79

---