Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4Q2B

The crystal structure of an endo-1,4-D-glucanase from Pseudomonas putida KT2440

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	0008810	molecular_function	cellulase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
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	0008810	molecular_function	cellulase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
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	0008810	molecular_function	cellulase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
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	0008810	molecular_function	cellulase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
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	0008810	molecular_function	cellulase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0000272	biological_process	polysaccharide catabolic process
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process
F	0008810	molecular_function	cellulase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	ARG177
A	HIS236

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 402

Chain	Residue
A	HOH677
A	HOH683
A	GLU55
A	ALA114
A	ASP116
A	TYR182
A	HOH529
A	HOH561
A	HOH617

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

Chain	Residue
A	ASN82
A	ASN83
A	HOH551
C	HOH649

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT A 404

Chain	Residue
A	ARG41

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT A 405

Chain	Residue
A	ARG190

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 401

Chain	Residue
B	ARG177
B	TRP221
B	LYS235
B	HIS236

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT B 402

Chain	Residue
B	ARG322
B	ASP348

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT B 403

Chain	Residue
B	GLN142
B	ARG190

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 401

Chain	Residue
C	ARG322
C	HOH640
D	ARG322
D	ASP348
D	ARG353

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 402

Chain	Residue
C	ARG177
C	LYS235
C	HIS236
C	IMD409

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MLA C 403

Chain	Residue
C	GLN142
C	TRP146
C	VAL194
C	HOH515
D	TRP146
D	HOH544
D	HOH666

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 404

Chain	Residue
C	VAL42
C	ILE43
C	ASP44
C	ILE51
C	THR52
C	THR53
C	GLY56

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 405

Chain	Residue
A	GLU263
A	HOH512
C	ARG41
C	ILE43

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT C 406

Chain	Residue
C	GLN260
C	ARG262
C	GLU263

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT C 407

Chain	Residue
C	LYS155
C	LEU156
C	GLU171
D	ARG154

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT C 408

Chain	Residue
C	ARG190

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD C 409

Chain	Residue
C	TRP96
C	TYR182
C	SO4402

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 401

Chain	Residue
D	ARG177
D	LYS235
D	HIS236

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 402

Chain	Residue
C	ARG322
C	ASP348
C	GLU349
D	ARG322
D	ASP348

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS D 403

Chain	Residue
D	GLU55
D	ALA114
D	ASP116
D	TYR182
D	HOH537
D	HOH557
D	HOH685

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT D 404

Chain	Residue
D	ARG190

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 401

Chain	Residue
E	ARG177
E	LYS235
E	HIS236

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS E 402

Chain	Residue
E	GLU55
E	ALA114
E	ASP116
E	TYR182
E	HOH513
E	HOH515
E	HOH579

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 401

Chain	Residue
F	ARG177
F	LYS235
F	HIS236

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS F 402

Chain	Residue
F	HOH587
F	HOH591
F	GLU55
F	TRP96
F	ALA114
F	ASP116
F	TYR182
F	ASP243
F	HOH522

Functional Information from PROSITE/UniProt

site_id	PS00812
Number of Residues	19
Details	GLYCOSYL_HYDROL_F8 Glycosyl hydrolases family 8 signature. ASDADlwIAySLLeAgrlW

Chain	Residue	Details
A	ALA114-TRP132

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)