Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NAL

THE THREE-DIMENSIONAL STRUCTURE OF N-ACETYLNEURAMINATE LYASE FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0005737	cellular_component	cytoplasm
1	0005829	cellular_component	cytosol
1	0005975	biological_process	carbohydrate metabolic process
1	0008747	molecular_function	N-acetylneuraminate lyase activity
1	0016829	molecular_function	lyase activity
1	0019262	biological_process	N-acetylneuraminate catabolic process
1	0042802	molecular_function	identical protein binding
1	0044010	biological_process	single-species biofilm formation
2	0005737	cellular_component	cytoplasm
2	0005829	cellular_component	cytosol
2	0005975	biological_process	carbohydrate metabolic process
2	0008747	molecular_function	N-acetylneuraminate lyase activity
2	0016829	molecular_function	lyase activity
2	0019262	biological_process	N-acetylneuraminate catabolic process
2	0042802	molecular_function	identical protein binding
2	0044010	biological_process	single-species biofilm formation
3	0005737	cellular_component	cytoplasm
3	0005829	cellular_component	cytosol
3	0005975	biological_process	carbohydrate metabolic process
3	0008747	molecular_function	N-acetylneuraminate lyase activity
3	0016829	molecular_function	lyase activity
3	0019262	biological_process	N-acetylneuraminate catabolic process
3	0042802	molecular_function	identical protein binding
3	0044010	biological_process	single-species biofilm formation
4	0005737	cellular_component	cytoplasm
4	0005829	cellular_component	cytosol
4	0005975	biological_process	carbohydrate metabolic process
4	0008747	molecular_function	N-acetylneuraminate lyase activity
4	0016829	molecular_function	lyase activity
4	0019262	biological_process	N-acetylneuraminate catabolic process
4	0042802	molecular_function	identical protein binding
4	0044010	biological_process	single-species biofilm formation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 1 302

Chain	Residue
1	ALA11
1	TYR43
1	GLY46
1	SER47
1	THR48
1	TYR137
1	LYS165

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 2 304

Chain	Residue
2	GLY46
2	SER47
2	THR48
2	TYR137
2	LYS165
2	ALA11
2	TYR43

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 3 306

Chain	Residue
3	ALA11
3	TYR43
3	GLY46
3	SER47
3	THR48
3	TYR137
3	LYS165

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 4 308

Chain	Residue
4	ALA11
4	TYR43
4	GLY46
4	SER47
4	THR48
4	TYR137
4	LYS165

Functional Information from PROSITE/UniProt

site_id	PS00665
Number of Residues	18
Details	DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGEAfvqslsE

Chain	Residue	Details
1	GLY41-GLU58

site_id	PS00666
Number of Residues	31
Details	DHDPS_2 Dihydrodipicolinate synthase signature 2. YNIPalSgvkLtldqintlvtlpg.VgALKQT

Chain	Residue	Details
1	TYR137-THR167

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"12711733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19923724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9047371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8081752","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9047371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12711733","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HL2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BWL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Site: {"description":"Required to correctly position the proton donor","evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
1	LEU142
1	TYR137
1	LYS165

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
2	LEU142
2	TYR137
2	LYS165

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
3	LEU142
3	TYR137
3	LYS165

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
4	LEU142
4	TYR137
4	LYS165

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
1	THR48
1	SER47
1	LYS165

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
2	THR48
2	SER47
2	LYS165

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
3	THR48
3	SER47
3	LYS165

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
4	THR48
4	SER47
4	LYS165

site_id	MCSA1
Number of Residues	2
Details	M-CSA 553

Chain

Residue

Details

site_id	MCSA2
Number of Residues	2
Details	M-CSA 553

Chain

Residue

Details

site_id	MCSA3
Number of Residues	2
Details	M-CSA 553

Chain

Residue

Details

site_id	MCSA4
Number of Residues	2
Details	M-CSA 553

Chain

Residue

Details

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