Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TEP

Crystal structure of a galactokinase from Bifidobacterium infantis in complex with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004335	molecular_function	galactokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006012	biological_process	galactose metabolic process
A	0016301	molecular_function	kinase activity
A	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
B	0004335	molecular_function	galactokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006012	biological_process	galactose metabolic process
B	0016301	molecular_function	kinase activity
B	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
C	0004335	molecular_function	galactokinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006012	biological_process	galactose metabolic process
C	0016301	molecular_function	kinase activity
C	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
D	0004335	molecular_function	galactokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006012	biological_process	galactose metabolic process
D	0016301	molecular_function	kinase activity
D	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PEG A 501

Chain	Residue
A	LYS69
A	PRO70
A	ARG71
A	GLU72
A	ASP73
A	ASP126

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 502

Chain	Residue
A	LYS323
A	TYR360
A	HOH640
A	GLY320
A	ASP321
A	ILE322

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL A 503

Chain	Residue
A	GLU46
A	HIS47
A	THR48
A	ASP49
A	TYR50
A	TYR248
A	HOH666
A	HOH773

site_id	AC4
Number of Residues	21
Details	binding site for residue ADP A 504

Chain	Residue
A	SER80
A	TRP103
A	TYR106
A	LEU135
A	GLY136
A	GLY138
A	SER140
A	SER141
A	SER142
A	MET145
A	MG507
A	HOH634
A	HOH641
A	HOH646
A	HOH658
A	HOH690
A	HOH693
A	HOH698
A	HOH754
A	HOH826
A	HOH835

site_id	AC5
Number of Residues	3
Details	binding site for residue CL A 505

Chain	Residue
A	ARG251
A	THR254
A	ARG299

site_id	AC6
Number of Residues	3
Details	binding site for residue CL A 506

Chain	Residue
A	ASP93
A	ARG115
A	HOH847

site_id	AC7
Number of Residues	5
Details	binding site for residue MG A 507

Chain	Residue
A	SER142
A	ADP504
A	HOH641
A	HOH690
A	HOH835

site_id	AC8
Number of Residues	5
Details	binding site for residue PEG D 501

Chain	Residue
D	ALA30
D	PRO31
D	GLU32
D	LYS69
D	PRO70

site_id	AC9
Number of Residues	4
Details	binding site for residue PEG D 502

Chain	Residue
D	LYS121
D	VAL156
D	TYR157
D	GLY158

site_id	AD1
Number of Residues	10
Details	binding site for residue PEG D 503

Chain	Residue
D	ARG40
D	GLY138
D	SER186
D	THR187
D	ASP191
D	TYR248
D	GLY366
D	GLY367
D	GOL504
D	HOH606

site_id	AD2
Number of Residues	10
Details	binding site for residue GOL D 504

Chain	Residue
D	GLU46
D	HIS47
D	ASP49
D	TYR50
D	THR187
D	GLY188
D	TYR248
D	PEG503
D	HOH692
D	HOH820

site_id	AD3
Number of Residues	21
Details	binding site for residue ADP D 505

Chain	Residue
D	HOH771
D	HOH779
D	HOH817
D	SER80
D	VAL82
D	TRP103
D	TYR106
D	LEU135
D	GLY136
D	GLY138
D	SER140
D	SER141
D	SER142
D	MET145
D	MG507
D	HOH606
D	HOH625
D	HOH638
D	HOH669
D	HOH719
D	HOH759

site_id	AD4
Number of Residues	3
Details	binding site for residue CL D 506

Chain	Residue
D	ARG251
D	THR254
D	ARG299

site_id	AD5
Number of Residues	4
Details	binding site for residue MG D 507

Chain	Residue
D	SER142
D	ADP505
D	HOH602
D	HOH625

site_id	AD6
Number of Residues	6
Details	binding site for residue PG4 C 501

Chain	Residue
C	THR343
C	VAL344
C	PRO345
C	GLU346
C	HOH636
C	HOH877

site_id	AD7
Number of Residues	5
Details	binding site for residue PEG C 502

Chain	Residue
C	GLY136
C	GLN238
C	ALA239
C	HIS241
C	HOH803

site_id	AD8
Number of Residues	9
Details	binding site for residue PEG C 503

Chain	Residue
C	ASP49
C	GLY188
C	GLY189
C	ASN193
C	CYS208
C	ASN217
C	HOH624
C	HOH831
C	HOH837

site_id	AD9
Number of Residues	4
Details	binding site for residue GOL C 504

Chain	Residue
C	GLN238
C	ALA400
C	HOH619
C	HOH825

site_id	AE1
Number of Residues	9
Details	binding site for residue GOL C 505

Chain	Residue
C	GLU46
C	HIS47
C	ASP49
C	TYR50
C	THR187
C	GLY188
C	TYR248
C	HOH711
C	HOH777

site_id	AE2
Number of Residues	7
Details	binding site for residue GOL C 506

Chain	Residue
A	LYS227
A	HOH608
A	HOH843
A	HOH928
C	ALA265
C	HOH612
C	HOH702

site_id	AE3
Number of Residues	24
Details	binding site for residue ADP C 507

Chain	Residue
C	SER80
C	VAL82
C	TRP103
C	TYR106
C	LEU135
C	GLY136
C	GLY138
C	SER140
C	SER141
C	SER142
C	MET145
C	MG509
C	HOH605
C	HOH609
C	HOH617
C	HOH631
C	HOH642
C	HOH656
C	HOH658
C	HOH659
C	HOH713
C	HOH717
C	HOH782
C	HOH859

site_id	AE4
Number of Residues	4
Details	binding site for residue CL C 508

Chain	Residue
C	GLN250
C	ARG251
C	THR254
C	ARG299

site_id	AE5
Number of Residues	6
Details	binding site for residue MG C 509

Chain	Residue
C	SER142
C	ADP507
C	HOH603
C	HOH609
C	HOH658
C	HOH713

site_id	AE6
Number of Residues	7
Details	binding site for residue PEG B 501

Chain	Residue
B	GLU294
B	LYS297
B	ARG301
B	HOH602
B	HOH603
B	HOH616
B	HOH707

site_id	AE7
Number of Residues	7
Details	binding site for residue PEG B 502

Chain	Residue
B	ARG77
B	VAL87
B	GLU89
B	HOH605
B	HOH636
B	HOH853
D	LYS395

site_id	AE8
Number of Residues	3
Details	binding site for residue PEG B 503

Chain	Residue
B	ASP163
B	HOH613
B	HOH639

site_id	AE9
Number of Residues	6
Details	binding site for residue PEG B 504

Chain	Residue
B	ASN193
B	ASN217
B	HOH610
B	HOH642
B	HOH655
B	HOH661

site_id	AF1
Number of Residues	7
Details	binding site for residue PEG B 505

Chain	Residue
B	GLY136
B	GLY138
B	GLN242
B	GLY368
B	PHE369
B	GLY371
B	HOH721

site_id	AF2
Number of Residues	5
Details	binding site for residue GOL B 506

Chain	Residue
B	LEU288
B	ASP289
B	LEU291
B	PRO292
B	LYS297

site_id	AF3
Number of Residues	5
Details	binding site for residue GOL B 507

Chain	Residue
B	ARG355
B	LYS356
B	ASN357
B	GLY358
B	HOH659

site_id	AF4
Number of Residues	8
Details	binding site for residue GOL B 508

Chain	Residue
B	GLU46
B	HIS47
B	ASP49
B	TYR50
B	LEU190
B	TYR248
B	HOH645
B	HOH798

site_id	AF5
Number of Residues	21
Details	binding site for residue ADP B 509

Chain	Residue
B	SER80
B	TRP103
B	TYR106
B	LEU135
B	GLY136
B	GLY138
B	SER140
B	SER141
B	SER142
B	MET145
B	MG511
B	HOH625
B	HOH665
B	HOH697
B	HOH700
B	HOH705
B	HOH721
B	HOH730
B	HOH796
B	HOH817
B	HOH820

site_id	AF6
Number of Residues	3
Details	binding site for residue CL B 510

Chain	Residue
B	ARG251
B	THR254
B	ARG299

site_id	AF7
Number of Residues	4
Details	binding site for residue MG B 511

Chain	Residue
B	SER142
B	ADP509
B	HOH700
B	HOH730

Functional Information from PROSITE/UniProt

site_id	PS00106
Number of Residues	12
Details	GALACTOKINASE Galactokinase signature. GRvNLIGEHtDY

Chain	Residue	Details
A	GLY39-TYR50

site_id	PS00627
Number of Residues	12
Details	GHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VPlGsGLSSSAA

Chain	Residue	Details
A	VAL133-ALA144

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