Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3IFS

2.0 Angstrom Resolution Crystal Structure of Glucose-6-phosphate Isomerase (pgi) from Bacillus anthracis.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004347	molecular_function	glucose-6-phosphate isomerase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0048029	molecular_function	monosaccharide binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0097367	molecular_function	carbohydrate derivative binding
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0004347	molecular_function	glucose-6-phosphate isomerase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0048029	molecular_function	monosaccharide binding
B	0051156	biological_process	glucose 6-phosphate metabolic process
B	0097367	molecular_function	carbohydrate derivative binding
B	1901135	biological_process	carbohydrate derivative metabolic process
C	0004347	molecular_function	glucose-6-phosphate isomerase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0048029	molecular_function	monosaccharide binding
C	0051156	biological_process	glucose 6-phosphate metabolic process
C	0097367	molecular_function	carbohydrate derivative binding
C	1901135	biological_process	carbohydrate derivative metabolic process
D	0004347	molecular_function	glucose-6-phosphate isomerase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0048029	molecular_function	monosaccharide binding
D	0051156	biological_process	glucose 6-phosphate metabolic process
D	0097367	molecular_function	carbohydrate derivative binding
D	1901135	biological_process	carbohydrate derivative metabolic process
E	0004347	molecular_function	glucose-6-phosphate isomerase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006094	biological_process	gluconeogenesis
E	0006096	biological_process	glycolytic process
E	0016853	molecular_function	isomerase activity
E	0048029	molecular_function	monosaccharide binding
E	0051156	biological_process	glucose 6-phosphate metabolic process
E	0097367	molecular_function	carbohydrate derivative binding
E	1901135	biological_process	carbohydrate derivative metabolic process
F	0004347	molecular_function	glucose-6-phosphate isomerase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006094	biological_process	gluconeogenesis
F	0006096	biological_process	glycolytic process
F	0016853	molecular_function	isomerase activity
F	0048029	molecular_function	monosaccharide binding
F	0051156	biological_process	glucose 6-phosphate metabolic process
F	0097367	molecular_function	carbohydrate derivative binding
F	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 451

Chain	Residue
A	SER105
A	LYS106
A	HOH508
A	HOH1330
A	HOH2001

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 451

Chain	Residue
B	HIS19
B	ARG173

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 452

Chain	Residue
B	SER144
B	LYS145
B	SER146
B	THR149
B	HOH518
B	HOH1286
B	HOH2073
A	HOH1865
B	SER85

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 453

Chain	Residue
B	ARG25
B	GLY168
B	LYS169
B	HOH1414

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE B 454

Chain	Residue
B	LYS71
B	ASN72
B	ASP73
B	SER74
B	ASP137
B	HOH2266

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LI C 451

Chain	Residue
C	HIS4
C	ASP240
C	HOH1214
F	GLU440

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 F 451

Chain	Residue
E	HIS36
E	HOH490
E	HOH1412
E	HOH1729
F	HIS36
F	HOH692
F	HOH770
F	HOH1224
F	HOH1302
F	HOH2143

Functional Information from PROSITE/UniProt

site_id	PS00174
Number of Residues	18
Details	P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GyLLgvnpFDQpGVEayK

Chain	Residue	Details
A	GLY409-LYS426

site_id	PS00765
Number of Residues	14
Details	P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DdVGGRFSVlTPVG

Chain	Residue	Details
A	ASP203-GLY216

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00473","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00473","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00473","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	GLY207
A	LYS426
A	GLU291
A	LYS145
A	ARG208
A	GLU151

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
D	HIS312

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
E	HIS312

site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
F	HIS312

site_id	CSA13
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	GLY207
A	GLU291
A	LYS435
A	LYS145
A	ARG208
A	GLU151

site_id	CSA14
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
B	GLY207
B	GLU291
B	LYS435
B	LYS145
B	ARG208
B	GLU151

site_id	CSA15
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
C	GLY207
C	GLU291
C	LYS435
C	LYS145
C	ARG208
C	GLU151

site_id	CSA16
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
D	GLY207
D	GLU291
D	LYS435
D	LYS145
D	ARG208
D	GLU151

site_id	CSA17
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
E	GLY207
E	GLU291
E	LYS435
E	LYS145
E	ARG208
E	GLU151

site_id	CSA18
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
F	GLY207
F	GLU291
F	LYS435
F	LYS145
F	ARG208
F	GLU151

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
B	GLY207
B	LYS426
B	GLU291
B	LYS145
B	ARG208
B	GLU151

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
C	GLY207
C	LYS426
C	GLU291
C	LYS145
C	ARG208
C	GLU151

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
D	GLY207
D	LYS426
D	GLU291
D	LYS145
D	ARG208
D	GLU151

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
E	GLY207
E	LYS426
E	GLU291
E	LYS145
E	ARG208
E	GLU151

site_id	CSA6
Number of Residues	6
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
F	GLY207
F	LYS426
F	GLU291
F	LYS145
F	ARG208
F	GLU151

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	HIS312

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
B	HIS312

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
C	HIS312

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