Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WID

Structure of a glucose dehydrogenase T277F mutant in complex with NADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005534	molecular_function	galactose binding
A	0005536	molecular_function	D-glucose binding
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0019595	biological_process	non-phosphorylated glucose catabolic process
A	0033498	biological_process	galactose catabolic process via D-galactonate
A	0046872	molecular_function	metal ion binding
A	0047910	molecular_function	galactose 1-dehydrogenase (NADP+) activity
A	0047934	molecular_function	glucose 1-dehydrogenase (NAD+) activity
A	0047935	molecular_function	glucose 1-dehydrogenase (NADP+) activity
A	0047936	molecular_function	glucose 1-dehydrogenase [NAD(P)+] activity
A	0051262	biological_process	protein tetramerization
A	0070401	molecular_function	NADP+ binding
A	0070403	molecular_function	NAD+ binding
B	0000166	molecular_function	nucleotide binding
B	0005534	molecular_function	galactose binding
B	0005536	molecular_function	D-glucose binding
B	0008270	molecular_function	zinc ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0019595	biological_process	non-phosphorylated glucose catabolic process
B	0033498	biological_process	galactose catabolic process via D-galactonate
B	0046872	molecular_function	metal ion binding
B	0047910	molecular_function	galactose 1-dehydrogenase (NADP+) activity
B	0047934	molecular_function	glucose 1-dehydrogenase (NAD+) activity
B	0047935	molecular_function	glucose 1-dehydrogenase (NADP+) activity
B	0047936	molecular_function	glucose 1-dehydrogenase [NAD(P)+] activity
B	0051262	biological_process	protein tetramerization
B	0070401	molecular_function	NADP+ binding
B	0070403	molecular_function	NAD+ binding
C	0000166	molecular_function	nucleotide binding
C	0005534	molecular_function	galactose binding
C	0005536	molecular_function	D-glucose binding
C	0008270	molecular_function	zinc ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0019595	biological_process	non-phosphorylated glucose catabolic process
C	0033498	biological_process	galactose catabolic process via D-galactonate
C	0046872	molecular_function	metal ion binding
C	0047910	molecular_function	galactose 1-dehydrogenase (NADP+) activity
C	0047934	molecular_function	glucose 1-dehydrogenase (NAD+) activity
C	0047935	molecular_function	glucose 1-dehydrogenase (NADP+) activity
C	0047936	molecular_function	glucose 1-dehydrogenase [NAD(P)+] activity
C	0051262	biological_process	protein tetramerization
C	0070401	molecular_function	NADP+ binding
C	0070403	molecular_function	NAD+ binding
D	0000166	molecular_function	nucleotide binding
D	0005534	molecular_function	galactose binding
D	0005536	molecular_function	D-glucose binding
D	0008270	molecular_function	zinc ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0019595	biological_process	non-phosphorylated glucose catabolic process
D	0033498	biological_process	galactose catabolic process via D-galactonate
D	0046872	molecular_function	metal ion binding
D	0047910	molecular_function	galactose 1-dehydrogenase (NADP+) activity
D	0047934	molecular_function	glucose 1-dehydrogenase (NAD+) activity
D	0047935	molecular_function	glucose 1-dehydrogenase (NADP+) activity
D	0047936	molecular_function	glucose 1-dehydrogenase [NAD(P)+] activity
D	0051262	biological_process	protein tetramerization
D	0070401	molecular_function	NADP+ binding
D	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	CYS99
A	CYS102
A	CYS110
A	ASP116

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAP A 1002

Chain	Residue
A	ASN216
A	ARG217
A	HIS218
A	TYR238
A	THR252
A	SER253
A	ASP255
A	THR258
A	PHE275
A	GLY276
A	PHE277
A	SER304
A	VAL305
A	ASP306
A	HOH1127
A	HOH1147
A	HOH1167
C	VAL295
A	ILE192
A	SER194
A	GLY195
A	SER196
A	GLU197

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGO A 1003

Chain	Residue
A	ARG95
A	LEU125
A	HIS126
A	ARG130
A	TYR134

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE A 1004

Chain	Residue
A	TYR82
A	ILE137
A	LEU140
A	VAL141
A	LYS142
A	LYS309
A	VAL313
B	ASP181
B	ILE185
B	GLY209

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1PE B 4001

Chain	Residue
A	ARG106
A	HOH1115
B	LYS173
B	GLN178
B	SER182
C	LYS173
C	ARG174

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 4002

Chain	Residue
B	CYS99
B	CYS102
B	CYS110
B	ASP116

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAP B 4003

Chain	Residue
B	ILE192
B	SER194
B	GLY195
B	SER196
B	GLU197
B	ASN216
B	ARG217
B	HIS218
B	TYR238
B	THR252
B	ASP255
B	THR258
B	PHE275
B	PHE277
B	SER304
B	VAL305
B	ASP306
B	HOH4125
B	HOH4129
B	HOH4197
D	VAL295

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGO B 4004

Chain	Residue
B	ARG95
B	ALA120
B	HIS126
B	ARG130
B	TYR134
B	HOH4170

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 1PE B 4005

Chain	Residue
A	GLN178
A	SER182
B	ARG106
B	GLU166
B	HIS311
B	GLN314
B	HOH4119
B	HOH4200
D	ARG174

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1PE B 4006

Chain	Residue
B	ASP317
B	HOH4145
A	ASP181
A	ILE185
B	ILE137
B	LEU140
B	VAL141
B	LYS142
B	ASN144
B	LYS309
B	VAL313
B	LEU316

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1001

Chain	Residue
C	CYS99
C	CYS102
C	CYS110
C	ASP116

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAP C 1002

Chain	Residue
A	VAL295
C	ILE192
C	GLY193
C	SER194
C	GLY195
C	SER196
C	GLU197
C	ASN216
C	ARG217
C	HIS218
C	TYR238
C	THR252
C	SER253
C	THR258
C	PHE275
C	PHE277
C	SER304
C	VAL305
C	ASP306
C	LYS349
C	HOH1129
C	HOH1131
C	HOH1147

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGO C 1003

Chain	Residue
C	ARG95
C	HIS126
C	ARG130
C	TYR134

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE C 1004

Chain	Residue
C	LEU140
C	VAL141
C	LYS142
C	ASN144
C	LYS309
C	VAL313
C	LEU316
C	ASP317
D	ASP181
D	ILE185

site_id	BC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE C 1005

Chain	Residue
B	LYS173
B	ARG174
C	LYS173
C	ILE176
C	GLN178
C	ASN179
C	SER182
C	HOH1155
D	ILE104
D	ARG106
D	GLU166

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE D 4001

Chain	Residue
A	LYS173
A	SER175
C	ILE104
C	ARG106
D	LYS173
D	ILE176
D	GLN178
D	ASN179
D	SER182
D	HOH4103
D	HOH4132

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 4002

Chain	Residue
D	CYS99
D	CYS102
D	CYS110
D	ASP116

site_id	BC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAP D 4003

Chain	Residue
B	VAL295
D	ASN160
D	ILE192
D	SER194
D	GLY195
D	SER196
D	GLU197
D	ASN216
D	ARG217
D	HIS218
D	TYR238
D	THR252
D	ASP255
D	THR258
D	PHE275
D	PHE277
D	SER304
D	VAL305
D	ASP306
D	HOH4114
D	HOH4158

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGO D 4004

Chain	Residue
D	ARG95
D	HIS126
D	PHE128
D	ARG130
D	TYR134
D	ASP135

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1PE D 4005

Chain	Residue
C	ASP181
C	ILE185
D	ILE137
D	LEU140
D	VAL141
D	LYS142
D	ASN144
D	LYS309
D	VAL313
D	LEU316
D	ASP317
D	HOH4166

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