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5UGV

DapB from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006520biological_processamino acid metabolic process
A0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0016597molecular_functionamino acid binding
A0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0019877biological_processdiaminopimelate biosynthetic process
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0070402molecular_functionNADPH binding
A0070404molecular_functionNADH binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006520biological_processamino acid metabolic process
B0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0016597molecular_functionamino acid binding
B0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0019877biological_processdiaminopimelate biosynthetic process
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0070402molecular_functionNADPH binding
B0070404molecular_functionNADH binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue NAD A 301
ChainResidue
AGLY7
ATHR77
AHOH419
ALYS9
AGLY10
ALYS11
AVAL12
AASP33
AALA34
APHE52
ATHR53

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS136
ASER141
AGLY142
ATHR143

site_idAC3
Number of Residues5
Detailsbinding site for residue PGE A 303
ChainResidue
AGLU195
ALEU197
ATHR206
BARG208
BASP210

site_idAC4
Number of Residues6
Detailsbinding site for residue PGE A 304
ChainResidue
ALEU131
ALEU190
AGLU195
AARG208
BGLU195
BTHR206

site_idAC5
Number of Residues21
Detailsbinding site for residue NAD B 301
ChainResidue
AGLU82
AGLN85
BGLY7
BLYS9
BGLY10
BLYS11
BVAL12
BASP33
BALA34
BPHE52
BTHR53
BVAL57
BGLY75
BTHR77
BALA102
BPRO103
BASN104
BPHE105
BHOH419
BHOH423
BHOH430

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AHIS132
BHIS132

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
ALYS136
BLYS136

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AGLY7
BGLY7

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12962488, ECO:0007744|PDB:1C3V
ChainResidueDetails
BGLY75
BALA102
ALYS11
ALYS136
BLYS11
BLYS136
AGLY75
AALA102

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12962488, ECO:0007744|PDB:1C3V, ECO:0007744|PDB:1P9L
ChainResidueDetails
BHIS133
BGLY142
AHIS133
AGLY142

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12962488, ECO:0000269|PubMed:20057050, ECO:0007744|PDB:1P9L, ECO:0007744|PDB:1YL7
ChainResidueDetails
AASP33
BASP33

219869

PDB entries from 2024-05-15

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