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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E46

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73S

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0005829	cellular_component	cytosol
P	0005996	biological_process	monosaccharide metabolic process
P	0006004	biological_process	fucose metabolic process
P	0008270	molecular_function	zinc ion binding
P	0008738	molecular_function	L-fuculose-phosphate aldolase activity
P	0016829	molecular_function	lyase activity
P	0016830	molecular_function	carbon-carbon lyase activity
P	0016832	molecular_function	aldehyde-lyase activity
P	0019317	biological_process	fucose catabolic process
P	0019323	biological_process	pentose catabolic process
P	0019568	biological_process	arabinose catabolic process
P	0019571	biological_process	D-arabinose catabolic process
P	0042355	biological_process	L-fucose catabolic process
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 S 300

Chain	Residue
P	ASN29
P	THR43
P	SER71
P	SER72
P	HOH406
P	HOH444
P	HOH411

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN S 999

Chain	Residue
P	HIS155
P	HOH478
P	HIS92
P	HIS94

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME S 314

Chain	Residue
P	CYS14
P	THR26
P	GLY28
P	THR41
P	HOH411

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:10821675, ECO:0000269\|PubMed:11054289

Chain	Residue	Details
P	SER73

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:11054289, ECO:0000269\|PubMed:8676381, ECO:0007744\|PDB:1E47, ECO:0007744\|PDB:1E48, ECO:0007744\|PDB:4FUA

Chain	Residue	Details
P	GLY28
P	THR43
P	SER71

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00987, ECO:0000269\|PubMed:10821675, ECO:0000269\|PubMed:11054289, ECO:0000269\|PubMed:15299567, ECO:0000269\|PubMed:8676381, ECO:0007744\|PDB:1DZU, ECO:0007744\|PDB:1DZV, ECO:0007744\|PDB:1DZW, ECO:0007744\|PDB:1DZX, ECO:0007744\|PDB:1DZY, ECO:0007744\|PDB:1DZZ, ECO:0007744\|PDB:1E48, ECO:0007744\|PDB:1E49, ECO:0007744\|PDB:1E4A, ECO:0007744\|PDB:1E4B, ECO:0007744\|PDB:1E4C, ECO:0007744\|PDB:1FUA, ECO:0007744\|PDB:2FUA, ECO:0007744\|PDB:3FUA, ECO:0007744\|PDB:4FUA

Chain	Residue	Details
P	SER73

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00987, ECO:0000269\|PubMed:10821675, ECO:0000269\|PubMed:11054289, ECO:0000269\|PubMed:15299567, ECO:0000269\|PubMed:8676381, ECO:0007744\|PDB:1DZU, ECO:0007744\|PDB:1DZV, ECO:0007744\|PDB:1DZW, ECO:0007744\|PDB:1DZX, ECO:0007744\|PDB:1DZY, ECO:0007744\|PDB:1DZZ, ECO:0007744\|PDB:1E46, ECO:0007744\|PDB:1E47, ECO:0007744\|PDB:1E48, ECO:0007744\|PDB:1E49, ECO:0007744\|PDB:1E4A, ECO:0007744\|PDB:1E4B, ECO:0007744\|PDB:1E4C, ECO:0007744\|PDB:1FUA, ECO:0007744\|PDB:2FUA, ECO:0007744\|PDB:3FUA, ECO:0007744\|PDB:4FUA

Chain	Residue	Details
P	HIS92
P	HIS94
P	HIS155

site_id	SWS_FT_FI5
Number of Residues	3
Details	SITE: Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269\|PubMed:10821675

Chain	Residue	Details
P	TYR113
P	PHE131
P	TYR209

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 72

Chain	Residue	Details
P	SER73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
P	HIS92	metal ligand
P	HIS94	metal ligand
P	TYR113	electrostatic stabiliser, transition state stabiliser
P	HIS155	metal ligand
P	TYR209	electrostatic stabiliser, transition state stabiliser

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