Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XMO

Human aldolase A I98F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003779	molecular_function	actin binding
A	0004332	molecular_function	fructose-bisphosphate aldolase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006000	biological_process	fructose metabolic process
A	0006096	biological_process	glycolytic process
A	0006754	biological_process	ATP biosynthetic process
A	0006941	biological_process	striated muscle contraction
A	0007015	biological_process	actin filament organization
A	0007339	biological_process	binding of sperm to zona pellucida
A	0008092	molecular_function	cytoskeletal protein binding
A	0008360	biological_process	regulation of cell shape
A	0015629	cellular_component	actin cytoskeleton
A	0015631	molecular_function	tubulin binding
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0031093	cellular_component	platelet alpha granule lumen
A	0031430	cellular_component	M band
A	0031674	cellular_component	I band
A	0034774	cellular_component	secretory granule lumen
A	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
A	0042802	molecular_function	identical protein binding
A	0045296	molecular_function	cadherin binding
A	0046716	biological_process	muscle cell cellular homeostasis
A	0051289	biological_process	protein homotetramerization
A	0061621	biological_process	canonical glycolysis
A	0061827	cellular_component	sperm head
A	0070061	molecular_function	fructose binding
A	0070062	cellular_component	extracellular exosome
A	1904724	cellular_component	tertiary granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0003723	molecular_function	RNA binding
B	0003779	molecular_function	actin binding
B	0004332	molecular_function	fructose-bisphosphate aldolase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0006000	biological_process	fructose metabolic process
B	0006096	biological_process	glycolytic process
B	0006754	biological_process	ATP biosynthetic process
B	0006941	biological_process	striated muscle contraction
B	0007015	biological_process	actin filament organization
B	0007339	biological_process	binding of sperm to zona pellucida
B	0008092	molecular_function	cytoskeletal protein binding
B	0008360	biological_process	regulation of cell shape
B	0015629	cellular_component	actin cytoskeleton
B	0015631	molecular_function	tubulin binding
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0031093	cellular_component	platelet alpha granule lumen
B	0031430	cellular_component	M band
B	0031674	cellular_component	I band
B	0034774	cellular_component	secretory granule lumen
B	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
B	0042802	molecular_function	identical protein binding
B	0045296	molecular_function	cadherin binding
B	0046716	biological_process	muscle cell cellular homeostasis
B	0051289	biological_process	protein homotetramerization
B	0061621	biological_process	canonical glycolysis
B	0061827	cellular_component	sperm head
B	0070061	molecular_function	fructose binding
B	0070062	cellular_component	extracellular exosome
B	1904724	cellular_component	tertiary granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue PO4 A 401

Chain	Residue
A	LEU271
A	SER272
A	GLY273
A	GLY303
A	ARG304

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 402

Chain	Residue
A	LYS200
A	GLN203
A	ARG259
B	LYS13

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 403

Chain	Residue
A	PHE80
A	HIS81
A	LYS108
A	ASP110
A	ARG134
A	TYR138

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 404

Chain	Residue
A	GLU166
A	ASN169
A	VAL170
B	LEU128
B	GLU166
B	ASN169

site_id	AC5
Number of Residues	4
Details	binding site for residue PO4 A 405

Chain	Residue
A	LYS13
B	LYS200
B	GLN203
B	ARG259

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL A 406

Chain	Residue
A	SER218
A	ILE222
A	LEU224
B	GLU207
B	LYS208
B	ARG259

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL B 401

Chain	Residue
A	GLU207
A	LYS208
A	ARG259
B	SER218
B	ILE222
B	LEU224
B	HOH507

site_id	AC8
Number of Residues	6
Details	binding site for residue PO4 B 402

Chain	Residue
B	LYS230
B	SER272
B	GLY273
B	GLY303
B	ARG304
B	TYR364

site_id	AC9
Number of Residues	1
Details	binding site for residue GOL B 403

Chain	Residue
B	PRO345

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL B 404

Chain	Residue
A	ALA211
A	LYS215
A	PRO262
B	ALA211
B	LYS215
B	THR260

Functional Information from PROSITE/UniProt

site_id	PS00158
Number of Residues	11
Details	ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN

Chain	Residue	Details
A	ILE222-ASN232

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Schiff-base intermediate with dihydroxyacetone-P","evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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