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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RO8

Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process
G	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
G	0005975	biological_process	carbohydrate metabolic process
H	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
H	0005975	biological_process	carbohydrate metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASP14
A	ALA296
A	ILE299
A	HOH611
A	HOH859
A	HOH895

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 402

Chain	Residue
A	TYR235
A	HOH508
A	GLU196
A	GLN232
A	GLY233

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 403

Chain	Residue
A	ASN182
A	PRO183
A	SER184
A	HOH609

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ASP14
B	ALA296
B	ILE299
B	HOH541
B	HOH640
B	HOH947

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 402

Chain	Residue
B	GLU196
B	GLN232
B	GLY233
B	TYR235
B	HOH882

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 403

Chain	Residue
B	THR60
B	PHE61
B	THR62
C	ASN243
C	HOH812

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	ASP14
C	ALA296
C	ILE299
C	HOH551
G	LEU273
G	PRO274

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 402

Chain	Residue
C	GLU196
C	GLN232
C	GLY233
C	TYR235
C	HOH941

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	ASP14
D	ALA296
D	ILE299
D	HOH775
D	HOH900

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 402

Chain	Residue
D	GLU196
D	GLN232
D	GLY233
D	TYR235

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	ASP14
E	ALA296
E	ILE299
E	HOH625
E	HOH866
E	HOH887

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 402

Chain	Residue
E	GLU196
E	GLN232
E	GLY233
E	TYR235
E	HOH809

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 403

Chain	Residue
A	ASN100
E	ASN141
E	GLN156

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 404

Chain	Residue
E	ASN141
E	PRO144
E	HOH545
E	HOH907

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 401

Chain	Residue
F	ASP14
F	ALA296
F	ILE299
F	HOH640
F	HOH823
F	HOH824

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 402

Chain	Residue
F	GLU196
F	GLN232
F	GLY233
F	TYR235
F	HOH874

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 401

Chain	Residue
G	ASP14
G	ALA296
G	ILE299
G	HOH574
G	HOH837
G	HOH892

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL G 402

Chain	Residue
G	GLU196
G	GLN232
G	GLY233
G	TYR235
G	HOH506

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 401

Chain	Residue
H	ASP14
H	ALA296
H	ILE299
H	HOH571
H	HOH615
H	HOH774

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL H 402

Chain	Residue
H	GLY233
H	TYR235
H	HOH829
H	GLU196
H	GLN232

Functional Information from PROSITE/UniProt

site_id	PS00591
Number of Residues	11
Details	GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVEVsVSELDV

Chain	Residue	Details
A	GLY255-VAL265

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	GLU138
B	GLU138
C	GLU138
D	GLU138
E	GLU138
F	GLU138
G	GLU138
H	GLU138

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ASP193
B	ASP193
C	ASP193
D	ASP193
E	ASP193
F	ASP193
G	ASP193
H	ASP193

site_id	SWS_FT_FI3
Number of Residues	8
Details	ACT_SITE: Nucleophile => ECO:0000255\|PROSITE-ProRule:PRU10061

Chain	Residue	Details
A	GLU262
B	GLU262
C	GLU262
D	GLU262
E	GLU262
F	GLU262
G	GLU262
H	GLU262

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PDB entries from 2024-07-10

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