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4DWB

Crystal structure of Trypanosoma cruzi farnesyl diphosphate synthase in complex with [2-(n-pentylamino)ethane-1,1-diyl]bisphosphonic acid and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004161molecular_functiondimethylallyltranstransferase activity
A0004337molecular_functiongeranyltranstransferase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0045337biological_processfarnesyl diphosphate biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IPE A 501
ChainResidue
AGLY47
AHOH610
AHOH612
ALYS48
ATYR49
APHE50
AARG51
AGLN91
APHE246
ALYS264
A0M7509

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AGLN21
AHIS141

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AASP191
AARG237
AGLU331
ASER334
ALEU335
AHOH653

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AHIS141
ATYR142
AHOH688

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 505
ChainResidue
AILE129
ALYS132
ALYS132
ASER133
AHOH625
AHOH633

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 506
ChainResidue
AASP98
AASP102
AASP170
AMG507
A0M7509
AHOH601
AHOH602
AHOH623

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 507
ChainResidue
AASP98
AASP102
AMG506
A0M7509
AHOH603
AHOH604

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 508
ChainResidue
AASP250
A0M7509
AHOH605
AHOH606
AHOH607

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 0M7 A 509
ChainResidue
ATYR94
AASP98
AASP102
AARG107
ATHR163
AGLN167
ALYS207
ATYR211
AASP250
ALYS264
AIPE501
AMG506
AMG507
AMG508
AHOH603
AHOH604
AHOH605
AHOH606
AHOH607
AHOH623

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGeyFQVqDDVmD
ChainResidueDetails
AILE242-ASP254

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVeDDim..DgsvmRRG
ChainResidueDetails
ALEU95-GLY109

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PDB entries from 2024-06-05

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