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4RCV

M. tuberculosis 1-deoxy-d-xylulose-5-phosphate reductoisomerase bound to 1-deoxy-L-erythrulose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008299biological_processisoprenoid biosynthetic process
A0016114biological_processterpenoid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A0030145molecular_functionmanganese ion binding
A0030604molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0051483biological_processterpenoid biosynthetic process, mevalonate-independent
A0051484biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process
A0070402molecular_functionNADPH binding
B0000287molecular_functionmagnesium ion binding
B0008299biological_processisoprenoid biosynthetic process
B0016114biological_processterpenoid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B0030145molecular_functionmanganese ion binding
B0030604molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
B0051483biological_processterpenoid biosynthetic process, mevalonate-independent
B0051484biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process
B0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP151
AGLU153
AGLU222
ADE2403

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NDP A 402
ChainResidue
AALA46
AGLY47
AGLY48
AALA49
AHIS50
AALA69
AALA103
ALEU104
ALEU108
AALA126
AASN127
ALYS128
AGLU129
AASP151
AASN209
AMET267
ADE2403
AHOH501
AHOH502
AHOH521
AHOH573
AGLY19
ATHR21
AGLY22
ASER23
AILE24

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DE2 A 403
ChainResidue
ALYS128
AASP151
ASER152
AGLU153
AASN209
ASER213
AASN218
AGLU222
AMN401
ANDP402

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO3 A 404
ChainResidue
AALA176
ASER177
ASER213
AASN218
ALYS219
AHOH538
AHOH544
AHOH562

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BASP151
BGLU153
BGLU222

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NDP B 402
ChainResidue
BGLY19
BTHR21
BGLY22
BSER23
BILE24
BGLY47
BGLY48
BALA49
BHIS50
BALA103
BLEU104
BVAL105
BHOH507

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO3 B 403
ChainResidue
BALA176
BSER177
BSER213
BASN218
BLYS219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00183
ChainResidueDetails
ATHR21
ASER152
AGLU153
ASER177
AHIS200
AGLY206
ASER213
AASN218
ALYS219
AGLU222
BTHR21
AGLY22
BGLY22
BSER23
BILE24
BGLY47
BASN127
BLYS128
BGLU129
BASP151
BSER152
BGLU153
ASER23
BSER177
BHIS200
BGLY206
BSER213
BASN218
BLYS219
BGLU222
AILE24
AGLY47
AASN127
ALYS128
AGLU129
AASP151

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PDB entries from 2024-05-01

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