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3DYF

T. Brucei Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-461 and Isopentyl Diphosphate

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
B0004161molecular_functiondimethylallyltranstransferase activity
B0004337molecular_functiongeranyltranstransferase activity
B0005737cellular_componentcytoplasm
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0045337biological_processfarnesyl diphosphate biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 3002
ChainResidue
AASP103
AASP107
AHOH5225

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 3003
ChainResidue
AASP255
AHOH5001

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 3004
ChainResidue
AHOH5003
AASP103
AASP107
AASP175
AHOH5002

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 4002
ChainResidue
BASP103
BASP107

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 4003
ChainResidue
BASP255
BHOH5161
BHOH5264

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 4004
ChainResidue
BASP103
BASP107
BASP175
BHOH5004

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NI9 A 3001
ChainResidue
ATYR99
AASP103
AASP107
AARG112
AGLN172
ALYS212
ATHR213
ATYR216
AGLN252
AASP255
ALYS269
AHOH5001
AHOH5003
AHOH5060
AHOH5143
AHOH5225

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NI9 B 4001
ChainResidue
BTYR99
BASP103
BASP107
BARG112
BGLN172
BLYS212
BTHR213
BASP255
BLYS269
BHOH5004
BHOH5116
BHOH5117
BHOH5161

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME B 9001
ChainResidue
BCYS159
BARG160
BARG163

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IPR B 6002
ChainResidue
BLYS47
BARG50
BGLN96
BARG113
BTYR216
BPHE251
BGLN252
BASP255
BARG365
BHOH5045
BHOH5112
BHOH5275

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE IPR A 6001
ChainResidue
AGLY46
ALYS47
AARG50
AGLN96
AARG113
ATYR216
ATHR217
APHE251
AGLN252
AASP255
AHOH5006
AHOH5022
AHOH5149
AHOH5151
AHOH5242
AHOH5252

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 7001
ChainResidue
AARG163
ATHR167
ATYR215
AHOH5294
BLYS24

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGeyFQVqDDVmD
ChainResidueDetails
AMET247-ASP259

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVeDDim..DnsvtRRG
ChainResidueDetails
ALEU100-GLY114

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PDB entries from 2024-06-12

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