5TJZ

Structure of 4-Hydroxytetrahydrodipicolinate Reductase from Mycobacterium tuberculosis with NADPH and 2,6 Pyridine Dicarboxylic Acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
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	0009274	cellular_component	peptidoglycan-based cell wall
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	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0070402	molecular_function	NADPH binding
A	0070404	molecular_function	NADH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PDC A 301

Chain	Residue
A	THR77
A	PHE217
A	NAP304
A	HOH424
A	HOH447
A	PRO103
A	ASN104
A	HIS133
A	LYS136
A	SER141
A	GLY142
A	THR143
A	ALA192

---

site_id	AC2
Number of Residues	8
Details	binding site for residue BEZ A 302

Chain	Residue
A	MET59
A	MET59
A	ARG83
A	ARG83
A	IMD303
A	IMD303
A	HOH494
A	HOH494

---

site_id	AC3
Number of Residues	10
Details	binding site for residue IMD A 303

Chain	Residue
A	MET59
A	MET59
A	GLY60
A	GLY60
A	GLU63
A	GLU63
A	TRP90
A	TRP90
A	BEZ302
A	BEZ302

---

site_id	AC4
Number of Residues	37
Details	binding site for residue NAP A 304

Chain	Residue
A	GLY7
A	LYS9
A	GLY10
A	LYS11
A	VAL12
A	LEU32
A	ASP33
A	ALA34
A	PHE52
A	THR53
A	GLY75
A	THR76
A	THR77
A	ALA102
A	PRO103
A	ASN104
A	PHE105
A	LYS136
A	PHE217
A	PDC301
A	EDO307
A	HOH402
A	HOH416
A	HOH421
A	HOH424
A	HOH440
A	HOH447
A	HOH449
A	HOH459
A	HOH480
A	HOH484
A	HOH491
A	HOH518
A	HOH522
A	HOH523
A	HOH563
A	HOH566

---

site_id	AC5
Number of Residues	9
Details	binding site for residue AE3 A 305

Chain	Residue
A	ILE129
A	LEU131
A	LEU190
A	GLU195
A	GLU195
A	THR204
A	ARG208
A	ASP210
A	HOH429

---

site_id	AC6
Number of Residues	4
Details	binding site for residue CL A 306

Chain	Residue
A	ARG146
A	LEU238
A	GLU239
A	HOH479

---

site_id	AC7
Number of Residues	9
Details	binding site for residue EDO A 307

Chain	Residue
A	THR53
A	HIS54
A	HIS135
A	LYS136
A	ALA137
A	NAP304
A	EDO308
A	HOH447
A	HOH459

---

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO A 308

Chain	Residue
A	HIS54
A	HIS135
A	EDO307
A	HOH416
A	HOH425
A	HOH454
A	HOH468

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO A 309

Chain	Residue
A	HOH487
A	HOH497
A	HOH602
A	GLU63
A	PHE64

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 310

Chain	Residue
A	GLY69
A	ASN96
A	THR97
A	HOH668

---

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO A 311

Chain	Residue
A	ASP138
A	ALA139
A	PRO140
A	THR167
A	HOH446
A	HOH499
A	HOH610

---

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO A 312

Chain	Residue
A	ASN161
A	HOH413

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO A 313

Chain	Residue
A	SO4315
A	HOH401
A	HOH510

---

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO A 314

Chain	Residue
A	PHE122
A	ASP124

---

site_id	AD6
Number of Residues	4
Details	binding site for residue SO4 A 315

Chain	Residue
A	LEU223
A	EDO313
A	HOH590
A	HOH591

---

site_id	AD7
Number of Residues	4
Details	binding site for residue CL A 316

Chain	Residue
A	LYS94
A	PRO95
A	ASN96
A	THR97

---

site_id	AD8
Number of Residues	2
Details	binding site for residue CL A 317

Chain	Residue
A	ALA81
A	LYS149

---

site_id	AD9
Number of Residues	7
Details	binding site for residue EDO A 318

Chain	Residue
A	ASP56
A	VAL57
A	HOH411
A	HOH454
A	HOH493
A	HOH522
A	HOH523

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU127-ALA144

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C3V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1C3V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P9L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20057050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P9L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YL7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---