3LCG

The D-sialic acid aldolase mutant V251L

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	10
Details	BINDING SITE FOR RESIDUE SO4 A 1912

Chain	Residue
A	ALA11
A	HOH1936
A	TYR43
A	GLY46
A	SER47
A	THR48
A	TYR137
A	LYS165
A	HOH381
A	HOH758

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 2053

Chain	Residue
A	SER168
A	GLY169
A	HOH426
A	HOH882
A	HOH890
A	HOH1819
A	HOH1823

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 1913

Chain	Residue
B	ALA11
B	TYR43
B	GLY46
B	SER47
B	THR48
B	TYR137
B	LYS165
B	HOH492
B	HOH496
B	HOH1846

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 2048

Chain	Residue
B	PRO140
B	SER168
B	GLY169
B	HOH547
B	HOH1271
B	HOH1273
B	HOH1275
B	HOH1834
B	HOH1919

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 C 1914

Chain	Residue
C	ALA11
C	TYR43
C	GLY46
C	SER47
C	THR48
C	TYR137
C	LYS165
C	HOH531
C	HOH617
C	HOH1241

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 2049

Chain	Residue
C	PRO140
C	SER168
C	GLY169
C	HOH651
C	HOH909
C	HOH927
C	HOH928
C	HOH1231
C	HOH1242

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 D 1915

Chain	Residue
D	ALA11
D	TYR43
D	GLY46
D	SER47
D	THR48
D	TYR137
D	LYS165
D	HOH673
D	HOH837
D	HOH1560

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 2050

Chain	Residue
D	SER168
D	GLY169
D	HOH552
D	HOH577
D	HOH1287
D	HOH1293

---

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	LYS165
B	LYS165
C	LYS165
D	LYS165

---

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	GLU192
C	SER208
D	THR167
D	GLY189
D	ASP191
D	GLU192
A	GLY189
D	SER208
A	ASP191
A	GLU192
A	SER208
B	THR167
B	GLY189
B	ASP191
B	GLU192

---

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	MCSA1
Number of Residues	2
Details	M-CSA 553

Chain	Residue	Details
A	TYR137	proton acceptor, proton donor, proton relay
A	LYS165	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	LYS165	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	LYS165	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	LYS165	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

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