5F1U

biomimetic design results in a potent allosteric inhibitor of dihydrodipicolinate synthase from Campylobacter jejuni

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
A	0009085	biological_process	lysine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0016829	molecular_function	lyase activity
A	0019877	biological_process	diaminopimelate biosynthetic process
A	0044281	biological_process	small molecule metabolic process
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
B	0009085	biological_process	lysine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0016829	molecular_function	lyase activity
B	0019877	biological_process	diaminopimelate biosynthetic process
B	0044281	biological_process	small molecule metabolic process
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
C	0009085	biological_process	lysine biosynthetic process
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
C	0016829	molecular_function	lyase activity
C	0019877	biological_process	diaminopimelate biosynthetic process
C	0044281	biological_process	small molecule metabolic process
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008652	biological_process	amino acid biosynthetic process
D	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
D	0009085	biological_process	lysine biosynthetic process
D	0009089	biological_process	lysine biosynthetic process via diaminopimelate
D	0016829	molecular_function	lyase activity
D	0019877	biological_process	diaminopimelate biosynthetic process
D	0044281	biological_process	small molecule metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue 3VN A 301

Chain	Residue
A	SER51
B	ALA52
B	LEU54
B	HIS56
B	HIS59
B	ASN84
B	GLU88
B	PHE110
B	EDO305
B	HOH403
B	HOH434
A	ALA52
A	LEU54
A	HIS59
A	ASN84
A	GLU88
A	PHE110
A	HOH441
B	SER51

---

site_id	AC2
Number of Residues	5
Details	binding site for residue PG4 A 302

Chain	Residue
A	GLN117
A	TYR120
A	ASP150
A	THR151
A	LYS154

---

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 303

Chain	Residue
A	ALA263
A	GLY264
A	GLY297

---

site_id	AC4
Number of Residues	1
Details	binding site for residue EDO A 304

Chain	Residue
A	GLY144

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 305

Chain	Residue
A	THR69
A	LYS71
A	THR73

---

site_id	AC6
Number of Residues	4
Details	binding site for residue CL B 301

Chain	Residue
B	GLY46
B	THR47
B	THR48
B	LYS166

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PGE B 302

Chain	Residue
B	GLN117
B	TYR120
B	THR151
B	LYS154

---

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO B 304

Chain	Residue
B	LYS32
B	THR69

---

site_id	AC9
Number of Residues	8
Details	binding site for residue EDO B 305

Chain	Residue
A	ALA52
A	LEU54
A	THR55
A	3VN301
B	HIS87
B	GLU88
B	HOH419
B	HOH441

---

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO C 301

Chain	Residue
C	CYS70
C	GLY72
C	THR73
C	VAL75
C	ASP102

---

site_id	AD2
Number of Residues	1
Details	binding site for residue EDO C 302

Chain	Residue
C	TYR261

---

site_id	AD3
Number of Residues	15
Details	binding site for residue 3VN D 301

Chain	Residue
C	SER51
C	ALA52
C	LEU54
C	HIS59
C	ASN84
C	GLU88
D	SER51
D	ALA52
D	LEU54
D	HIS59
D	ASN84
D	GLU88
D	PHE110
D	HOH405
D	HOH423

---

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO D 302

Chain	Residue
D	TYR261
D	LEU262

---

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO D 303

Chain	Residue
D	ASP150
D	THR151
D	LYS154

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA41-GLU58

---

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

Chain	Residue	Details
A	TYR137-ALA168

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Part of a proton relay during catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---