Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2CXN

Crystal structure of mouse AMF / phosphate complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001701	biological_process	in utero embryonic development
A	0001707	biological_process	mesoderm formation
A	0002639	biological_process	positive regulation of immunoglobulin production
A	0004347	molecular_function	glucose-6-phosphate isomerase activity
A	0005125	molecular_function	cytokine activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0007165	biological_process	signal transduction
A	0007611	biological_process	learning or memory
A	0008083	molecular_function	growth factor activity
A	0010595	biological_process	positive regulation of endothelial cell migration
A	0016853	molecular_function	isomerase activity
A	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032355	biological_process	response to estradiol
A	0032570	biological_process	response to progesterone
A	0033574	biological_process	response to testosterone
A	0034101	biological_process	erythrocyte homeostasis
A	0035902	biological_process	response to immobilization stress
A	0035994	biological_process	response to muscle stretch
A	0042593	biological_process	glucose homeostasis
A	0043066	biological_process	negative regulation of apoptotic process
A	0043209	cellular_component	myelin sheath
A	0046686	biological_process	response to cadmium ion
A	0048029	molecular_function	monosaccharide binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0060170	cellular_component	ciliary membrane
A	0061620	biological_process	glycolytic process through glucose-6-phosphate
A	0061621	biological_process	canonical glycolysis
A	0097367	molecular_function	carbohydrate derivative binding
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0001701	biological_process	in utero embryonic development
B	0001707	biological_process	mesoderm formation
B	0002639	biological_process	positive regulation of immunoglobulin production
B	0004347	molecular_function	glucose-6-phosphate isomerase activity
B	0005125	molecular_function	cytokine activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0007165	biological_process	signal transduction
B	0007611	biological_process	learning or memory
B	0008083	molecular_function	growth factor activity
B	0010595	biological_process	positive regulation of endothelial cell migration
B	0016853	molecular_function	isomerase activity
B	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032355	biological_process	response to estradiol
B	0032570	biological_process	response to progesterone
B	0033574	biological_process	response to testosterone
B	0034101	biological_process	erythrocyte homeostasis
B	0035902	biological_process	response to immobilization stress
B	0035994	biological_process	response to muscle stretch
B	0042593	biological_process	glucose homeostasis
B	0043066	biological_process	negative regulation of apoptotic process
B	0043209	cellular_component	myelin sheath
B	0046686	biological_process	response to cadmium ion
B	0048029	molecular_function	monosaccharide binding
B	0051156	biological_process	glucose 6-phosphate metabolic process
B	0060170	cellular_component	ciliary membrane
B	0061620	biological_process	glycolytic process through glucose-6-phosphate
B	0061621	biological_process	canonical glycolysis
B	0097367	molecular_function	carbohydrate derivative binding
B	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 1601

Chain	Residue
A	SER160
A	SER210
A	LYS211
A	THR212
A	THR215
A	HOH1707
A	HOH1847
A	HOH1916
A	HOH1995

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1701

Chain	Residue
A	ASP140
A	TRP141
A	LYS142
A	LYS241
A	HOH1950
A	HOH2302

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1702

Chain	Residue
A	ILE549
A	ARG553
B	GLY419
B	HIS422
B	LYS423
B	LEU426
B	HOH1926
B	HOH1947

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1703

Chain	Residue
B	ARG135
B	TRP141
B	LYS142
B	HOH1857

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1704

Chain	Residue
A	GLY419
A	HIS422
A	LYS423
A	LEU426
A	HOH1839
A	HOH1956
B	ARG553

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY502-LYS519

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

Chain	Residue	Details
A	ASP268-GLY281

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16375918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U0F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	HIS389
B	GLY272
B	ARG273
B	LYS211
B	GLU358
B	LYS519
B	GLU217

site_id	CSA2
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	GLY272
A	ARG273
A	LYS211
A	LYS519
A	GLU358
A	GLU217
B	HIS389

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)