Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XFW

Structure of the E192N mutant of E. coli N-acetylneuraminic acid lyase in complex with pyruvate in crystal form III

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PYR B 1297

Chain	Residue
B	TYR190
B	ASP191
B	ASN192
B	HOH2172

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PYR A 1298

Chain	Residue
A	TYR190
A	ASP191
A	ASN192
A	SER208
A	HOH2256

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PYR D 1298

Chain	Residue
D	GLY189
D	TYR190
D	ASP191
D	ASN192
D	SER208
D	HOH2256
D	HOH2257

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PYR C 1298

Chain	Residue
C	TYR190
C	ASP191
C	ASN192
C	HOH2173
C	HOH2175

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PYR C 1299

Chain	Residue
B	LEU142
B	HOH2107
C	ALA141
C	GLY144
C	HOH2116

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PYR C 1300

Chain	Residue
C	LYS234
C	LEU235
C	GLU238
C	GLU295

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE 1PE A 1299

Chain	Residue
A	ASP263

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE 1PE D 1299

Chain	Residue
D	GLN37
D	GLU295

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE A 1300

Chain	Residue
A	LYS73
A	LYS75
A	ASP101

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE D 1300

Chain	Residue
A	PRO140
A	ALA141
A	GLY144
D	PRO140
D	ALA141
D	GLY144

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY41-GLU58

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

Chain	Residue	Details
A	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	MCSA1
Number of Residues	2
Details	M-CSA 553

Chain	Residue	Details
A	TYR137	proton acceptor, proton donor, proton relay
A	KPI165	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_id	MCSA2
Number of Residues	2
Details	M-CSA 553

Chain	Residue	Details
B	TYR137	proton acceptor, proton donor, proton relay
B	KPI165	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_id	MCSA3
Number of Residues	2
Details	M-CSA 553

Chain	Residue	Details
C	TYR137	proton acceptor, proton donor, proton relay
C	KPI165	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_id	MCSA4
Number of Residues	2
Details	M-CSA 553

Chain	Residue	Details
D	TYR137	proton acceptor, proton donor, proton relay
D	KPI165	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

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