2WKJ

Crystal structure of the E192N mutant of E. Coli N-acetylneuraminic acid lyase in complex with pyruvate at 1.45A resolution in space group P212121

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	6
Details	BINDING SITE FOR RESIDUE 1PE A 1297

Chain	Residue
A	LEU282
A	PRO283
A	LYS286
C	GLN36
C	GLN37
C	GLY38

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PYR C 1298

Chain	Residue
C	ASN192
C	SER208
C	THR209
C	HOH2339
C	HOH2340
C	GLY189
C	TYR190
C	ASP191

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PYR D 1297

Chain	Residue
D	GLY189
D	TYR190
D	ASP191
D	ASN192
D	ILE243
D	HOH2274
D	HOH2275

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR CHAIN C OF RESIDUES 1297 TO 1297

Chain	Residue
C	GLN36
C	GLN37
C	GLY38

---

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	ACT_SITE: Proton donor => ECO:0000305|PubMed:24521460

Chain	Residue	Details
A	TYR137
B	TYR137
C	TYR137
D	TYR137

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752

Chain	Residue	Details
A	KPI165
B	KPI165
C	KPI165
D	KPI165

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2

Chain	Residue	Details
A	SER47
A	THR48
B	SER47
B	THR48
C	SER47
C	THR48
D	SER47
D	THR48

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL

Chain	Residue	Details
A	THR167
B	SER208
C	THR167
C	GLY189
C	ASP191
C	ASN192
C	SER208
D	THR167
D	GLY189
D	ASP191
D	ASN192
A	GLY189
D	SER208
A	ASP191
A	ASN192
A	SER208
B	THR167
B	GLY189
B	ASP191
B	ASN192

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	SITE: Required to correctly position the proton donor => ECO:0000305|PubMed:24521460

Chain	Residue	Details
A	SER47
A	TYR110
B	SER47
B	TYR110
C	SER47
C	TYR110
D	SER47
D	TYR110

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1fdy

Chain	Residue	Details
A	THR48
A	SER47

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1fdy

Chain	Residue	Details
B	THR48
B	SER47

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fdy

Chain	Residue	Details
C	THR48
C	SER47

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1fdy

Chain	Residue	Details
D	THR48
D	SER47

---

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

---