Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4A03

Crystal Structure of Mycobacterium tuberculosis DXR in complex with the antibiotic FR900098 and cofactor NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008299biological_processisoprenoid 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
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 Residues5
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
ALYS128
AASP151
AGLU153
AGLU222
AF98501

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE F98 A 501
ChainResidue
AALA176
ASER177
AHIS200
ATRP203
AMET205
AASN209
ASER213
AASN218
ALYS219
AGLU222
AMN401
ANDP601
AHOH2143
AHOH2144
AHOH2185
ALYS128
AASP151
ASER152
AGLU153

site_idAC3
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NDP A 601
ChainResidue
AGLY19
ASER20
ATHR21
AGLY22
ASER23
AILE24
AALA46
AGLY47
AGLY48
AALA49
AHIS50
AALA69
AALA103
ALEU104
ALEU108
AALA126
AASN127
ALYS128
AGLU129
AASP151
AMET205
AGLY206
AASN209
AMET267
AF98501
AHOH2003
AHOH2008
AHOH2030
AHOH2035
AHOH2074
AHOH2114
AHOH2178
AHOH2179
AHOH2296
AHOH2297
AHOH2298
AHOH2299
AHOH2300
AHOH2301

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
ATHR64
AASN65
APRO81
ATYR82
ALYS171
AASP235
AILE237
AASP238
AARG313

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BLYS128
BASP151
BGLU153
BGLU222
BF98501

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE F98 B 501
ChainResidue
BLYS128
BASP151
BSER152
BGLU153
BALA176
BSER177
BHIS200
BTRP203
BMET205
BASN209
BSER213
BASN218
BLYS219
BGLU222
BMN401
BNDP601
BHOH2105
BHOH2106
BHOH2148

site_idAC7
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP B 601
ChainResidue
BSER23
BILE24
BALA46
BGLY47
BGLY48
BALA49
BHIS50
BALA69
BALA103
BLEU104
BLEU108
BALA126
BASN127
BLYS128
BGLU129
BASP151
BMET205
BGLY206
BASN209
BMET267
BF98501
BHOH2001
BHOH2006
BHOH2007
BHOH2024
BHOH2046
BHOH2078
BHOH2142
BHOH2143
BHOH2227
BGLY19
BTHR21
BGLY22

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon