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1Q0L

Crystal structure of DXR in complex with fosmidomycin

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051484biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process
A0070402molecular_functionNADPH binding
A1990065cellular_componentDxr protein complex
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FOM A 399
ChainResidue
ASER151
AGLU231
ANDP400
AHOH422
AHOH433
AHOH434
AGLU152
AGLY185
ASER186
AGLY187
AILE218
ASER222
AASN227
ALYS228

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP A 400
ChainResidue
AGLY8
ATHR10
AGLY11
ASER12
AILE13
AALA35
AGLY36
ALYS37
AASN38
AASP57
AALA100
AILE101
AVAL102
AALA105
AALA123
AASN124
ALYS125
AGLU126
AASP150
AMET214
AGLY215
AILE218
AMET276
AFOM399
AHOH403
AHOH460
AHOH483

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBINDING: BINDING => ECO:0000269|PubMed:15567415, ECO:0007744|PDB:1Q0Q
ChainResidueDetails
ATHR10
AGLU126
ASER151
ASER186
AHIS209
AGLY215
ASER222
AASN227
ALYS228
AGLY11
ASER12
AILE13
AGLY36
ALYS37
AASN38
AASN124
ALYS125

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12621040, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP
ChainResidueDetails
AASP150
AGLU152
AGLU231

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PDB entries from 2024-07-24

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