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5TJY

Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Mycobacterium tuberculosis with 2,6 Pyridine Dicarboxylic Acid and NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016491molecular_functionoxidoreductase activity
A0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A0019877biological_processdiaminopimelate biosynthetic process
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PDC A 301
ChainResidue
ATHR77
ANAI302
AHOH413
AHOH420
APRO103
AASN104
AHIS133
ALYS136
ASER141
AGLY142
ATHR143
AALA192

site_idAC2
Number of Residues26
Detailsbinding site for residue NAI A 302
ChainResidue
AGLY7
ALYS9
AGLY10
ALYS11
AVAL12
AASP33
AALA34
APHE52
ATHR53
AVAL57
AGLY75
ATHR76
ATHR77
AALA102
APRO103
AASN104
APHE105
ALYS136
AASP138
APHE217
APDC301
AHOH404
AHOH410
AHOH413
AHOH420
AHOH429

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLY78
AALA139
APRO140
AHOH401

site_idAC4
Number of Residues8
Detailsbinding site for residue BEZ A 304
ChainResidue
AMET59
AMET59
AARG83
AARG83
AIMD305
AIMD305
AHOH418
AHOH418

site_idAC5
Number of Residues9
Detailsbinding site for residue IMD A 305
ChainResidue
AMET59
AMET59
AGLY60
AGLY60
AGLU63
AGLU63
ATRP90
ABEZ304
ABEZ304

site_idAC6
Number of Residues6
Detailsbinding site for residue PG4 A 306
ChainResidue
AGLU195
AGLU195
ATHR206
AARG208
AASP210
AASP210

site_idAC7
Number of Residues5
Detailsbinding site for residue NA A 307
ChainResidue
AVAL20
AALA21
AALA23
ALEU26
AHOH491

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO A 308
ChainResidue
APHE122

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 309
ChainResidue
AASN45

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 310
ChainResidue
AARG173
AGLY174
AASP176
APRO181

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO A 312
ChainResidue
AASP176
AASP178
AGLY179

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO A 313
ChainResidue
AASN161
AASP163

site_idAD4
Number of Residues4
Detailsbinding site for residue CL A 314
ChainResidue
AGLY237
ALEU238
AGLU239
AHOH433

Functional Information from PROSITE/UniProt
site_idPS01298
Number of Residues18
DetailsDAPB Dihydrodipicolinate reductase signature. EViElHhphKaDapSGTA
ChainResidueDetails
AGLU127-ALA144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AHIS132

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
ALYS136

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AGLY75
AALA102
AHIS133
AGLY142
AGLY7

219869

PDB entries from 2024-05-15

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