2DCY

Crystal structure of Bacillus subtilis family-11 xylanase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031176	molecular_function	endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031176	molecular_function	endo-1,4-beta-xylanase activity
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	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	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
E	0000272	biological_process	polysaccharide catabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0031176	molecular_function	endo-1,4-beta-xylanase activity
E	0045493	biological_process	xylan catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO C 601

Chain	Residue
C	TRP9
C	TYR69
C	PRO116
C	SER117
C	TYR166
C	HOH638

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DIO A 602

Chain	Residue
B	TRP30
A	ASN29
A	TRP30
B	ASN29

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DIO B 603

Chain	Residue
A	ILE15
A	ASN17
A	ASN29
A	TRP30
A	SER31
B	ILE15
B	ASN17
B	ASN29
B	TRP30
B	SER31

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TAR E 501

Chain	Residue
A	SER134
A	LYS135
E	SER74
E	LYS99
E	SER100
E	ASP101
E	GLY102
E	GLY103
E	HOH528

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TAR B 502

Chain	Residue
B	ASN8
B	VAL16
B	ASN17
B	ALA18
B	TYR113
B	TLA505

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TAR B 503

Chain	Residue
A	GLN175
A	SER176
A	HOH610
B	TYR65
B	TYR88
B	PRO90
B	THR91
B	THR110
B	ARG112
B	GLN127
B	TRP129
B	HOH630
B	HOH633
B	HOH639

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TAR A 504

Chain	Residue
A	SER100
A	ASP101
A	GLY102
A	ASN148

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TAR B 505

Chain	Residue
B	TRP6
B	ASN8
B	ALA18
B	TYR113
B	TLA502
C	SER134
C	LYS135
C	HOH644

---

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TAR C 506

Chain	Residue
A	ALA1
C	THR3
C	ASP4
C	TYR5
C	ASN20
C	SER22
C	GLY23
C	GLY24
C	LYS40
C	HOH634

---

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAR A 507

Chain	Residue
A	TRP58
A	SER84
A	TRP85
A	LYS135
A	HOH607
A	HOH619
A	HOH626
E	VAL98
E	ASN148
E	ASN151
E	ALA152

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO75-TRP85

---

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

Chain	Residue	Details
A	MET169-SER180

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	920
Details	Domain: {"description":"GH11","evidences":[{"source":"PROSITE-ProRule","id":"PRU01097","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10062","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7911679","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10063","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bvv

Chain	Residue	Details
A	GLU172
A	GLU78

---

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

Chain	Residue	Details
B	GLU172
B	GLU78

---

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

Chain	Residue	Details
C	GLU172
C	GLU78

---

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

Chain	Residue	Details
D	GLU172
D	GLU78

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bvv

Chain	Residue	Details
E	GLU172
E	GLU78

---