Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ARZ

ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE

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	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
A	0009085	biological_process	lysine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0016491	molecular_function	oxidoreductase activity
A	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A	0019877	biological_process	diaminopimelate biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
B	0009085	biological_process	lysine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0016491	molecular_function	oxidoreductase activity
B	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
B	0019877	biological_process	diaminopimelate biosynthetic process
B	0042802	molecular_function	identical protein binding
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
C	0009085	biological_process	lysine biosynthetic process
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
C	0016491	molecular_function	oxidoreductase activity
C	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
C	0019877	biological_process	diaminopimelate biosynthetic process
C	0042802	molecular_function	identical protein binding
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008652	biological_process	amino acid biosynthetic process
D	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
D	0009085	biological_process	lysine biosynthetic process
D	0009089	biological_process	lysine biosynthetic process via diaminopimelate
D	0016491	molecular_function	oxidoreductase activity
D	0016726	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
D	0019877	biological_process	diaminopimelate biosynthetic process
D	0042802	molecular_function	identical protein binding
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 301

Chain	Residue
A	HIS160
A	LYS163
A	VAL217
A	ARG240

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 301

Chain	Residue
B	ALA25
B	LEU26
B	LEU28
B	VAL31
B	HOH411

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAI B 302

Chain	Residue
B	GLY12
B	GLY14
B	GLY15
B	ARG16
B	MET17
B	GLU38
B	PHE79
B	THR80
B	ARG81
B	GLY84
B	HIS88
B	GLY102
B	THR104
B	ALA127
B	ASN128
B	PHE129
B	LYS163
B	PHE243
B	PDC303
B	HOH415
B	HOH425

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDC B 303

Chain	Residue
B	THR104
B	ALA127
B	HIS160
B	LYS163
B	SER168
B	GLY169
B	THR170
B	NAI302
B	HOH425
B	HOH435

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAI C 301

Chain	Residue
B	HOH404
C	GLY12
C	GLY15
C	ARG16
C	MET17
C	GLU38
C	PHE79
C	THR80
C	ARG81
C	GLY84
C	GLY102
C	THR103
C	THR104
C	ALA127
C	PHE129
C	LYS163
C	PHE243
C	PDC302
C	HOH406
C	HOH410
C	HOH422
C	HOH423
C	HOH439

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PDC C 302

Chain	Residue
C	THR104
C	ALA127
C	HIS160
C	LYS163
C	SER168
C	GLY169
C	THR170
C	NAI301
C	HOH439

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D 301

Chain	Residue
D	ASP3
D	ALA25
D	LEU26
D	LEU28
D	VAL31

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAI D 302

Chain	Residue
D	HOH440
D	GLY12
D	GLY14
D	GLY15
D	ARG16
D	MET17
D	GLU38
D	ARG39
D	PHE79
D	THR80
D	ARG81
D	GLY84
D	GLY102
D	THR103
D	THR104
D	ALA127
D	ASN128
D	PHE129
D	LYS163
D	PHE243
D	PDC303
D	HOH426
D	HOH433

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PDC D 303

Chain	Residue
D	THR104
D	ALA127
D	HIS160
D	LYS163
D	SER168
D	GLY169
D	THR170
D	NAI302
D	HOH413
D	HOH415
D	HOH433

Functional Information from PROSITE/UniProt

site_id	PS01298
Number of Residues	18
Details	DAPB Dihydrodipicolinate reductase signature. EIiEaHhrhKvDapSGTA

Chain	Residue	Details
A	GLU154-ALA171

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7893645","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DIH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8873595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ARZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DRU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9398235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ARZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9398235

Chain	Residue	Details
A	LYS163
A	HIS159

site_id	MCSA1
Number of Residues	2
Details	M-CSA 402

Chain	Residue	Details
A	HIS159	activator, proton shuttle (general acid/base)
A	LYS163	activator, electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	2
Details	M-CSA 402

Chain	Residue	Details
B	HIS159	activator, proton shuttle (general acid/base)
B	LYS163	activator, electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	2
Details	M-CSA 402

Chain	Residue	Details
C	HIS159	activator, proton shuttle (general acid/base)
C	LYS163	activator, electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	2
Details	M-CSA 402

Chain	Residue	Details
D	HIS159	activator, proton shuttle (general acid/base)
D	LYS163	activator, electrostatic stabiliser, proton shuttle (general acid/base)

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