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1YL6

crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) (crystal form B)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009274cellular_componentpeptidoglycan-based cell wall
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
A0070402molecular_functionNADPH binding
A0070404molecular_functionNADH binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 246
ChainResidue
AVAL20
AALA21
AALA23
ALEU26

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 246
ChainResidue
BVAL20
BALA21
BALA23
BLEU26

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

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12962488, ECO:0000269|PubMed:20057050, ECO:0007744|PDB:1P9L, ECO:0007744|PDB:1YL7
ChainResidueDetails
AASP33
BASP33

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

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PDB entries from 2024-06-12

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