3N2X

Crystal structure of YagE, a prophage protein belonging to the dihydrodipicolinic acid synthase family from E. coli K12 in complex with pyruvate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0016829	molecular_function	lyase activity
A	0042802	molecular_function	identical protein binding
A	0046176	biological_process	aldonic acid catabolic process
A	0047440	molecular_function	2-dehydro-3-deoxy-D-pentonate aldolase activity
A	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0016829	molecular_function	lyase activity
B	0042802	molecular_function	identical protein binding
B	0046176	biological_process	aldonic acid catabolic process
B	0047440	molecular_function	2-dehydro-3-deoxy-D-pentonate aldolase activity
B	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0016829	molecular_function	lyase activity
C	0042802	molecular_function	identical protein binding
C	0046176	biological_process	aldonic acid catabolic process
C	0047440	molecular_function	2-dehydro-3-deoxy-D-pentonate aldolase activity
C	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0016829	molecular_function	lyase activity
D	0042802	molecular_function	identical protein binding
D	0046176	biological_process	aldonic acid catabolic process
D	0047440	molecular_function	2-dehydro-3-deoxy-D-pentonate aldolase activity
D	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 1

Chain	Residue
A	LEU54
A	TYR145
A	PHE60
A	ARG68
A	GLY88
A	THR89
A	GLY90
A	VAL113
A	VAL114
A	ILE115

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO B 2

Chain	Residue
B	LEU54
B	PHE60
B	ARG68
B	GLY88
B	THR89
B	GLY90
B	VAL113
B	VAL114
B	ILE115

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO C 3

Chain	Residue
C	LEU54
C	PHE60
C	ARG68
C	GLY88
C	THR89
C	GLY90
C	VAL113
C	VAL114
C	ILE115
C	TYR145

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO D 4

Chain	Residue
D	LEU54
D	PHE60
D	ARG68
D	GLY88
D	GLY90
D	VAL113
D	VAL114
D	ILE115
D	TYR145

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY50-GLU67

---

site_id	PS00666
Number of Residues	32
Details	DHDPS_2 Dihydrodipicolinate synthase signature 2. YNFPalTgqdLtpalvktladsrsnIiGIKDT

Chain	Residue	Details
A	TYR145-THR176

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:21294156

Chain	Residue	Details
A	ASP49
A	ILE112
B	ASP49
B	ILE112
C	ASP49
C	ILE112
D	ASP49
D	ILE112

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21294156

Chain	Residue	Details
A	VAL138
B	VAL138
C	VAL138
D	VAL138

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	ACT_SITE: Schiff-base intermediate with substrate => ECO:0000305|PubMed:21294156

Chain	Residue	Details
A	ARG167
B	ARG167
C	ARG167
D	ARG167

---