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4Q23

The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0008299biological_processisoprenoid biosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE RIS A 901
ChainResidue
ALEU100
AMG903
AMG904
AHOH1001
AHOH1003
AHOH1088
AHOH1089
AHOH1092
AHOH1093
AHOH1094
AHOH1096
AASP103
AASP107
AARG112
AGLN171
ALYS200
AASP243
ALYS257
AMG902

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AASP103
AASP107
ARIS901
AMG904
AHOH1090
AHOH1092

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 903
ChainResidue
AASP243
ARIS901
AHOH1088
AHOH1089
AHOH1093

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 904
ChainResidue
AASP103
AASP107
ARIS901
AMG902
AHOH1094
AHOH1095
AHOH1096

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 905
ChainResidue
AGLY56
ALYS57
AGLN96
AARG113
AHOH1016
AHOH1056
AHOH1099
AHOH1119

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD
ChainResidueDetails
AMET235-ASP247

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG
ChainResidueDetails
ALEU100-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
ChainResidueDetails
ALYS57
AARG60
AGLN96
AASP103
AASP107
AARG113

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AARG112
ALYS200
AALA201
AGLN240
ALYS257

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS266

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for determining product chain length => ECO:0000250
ChainResidueDetails
APHE98
APHE99

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS57

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS287

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PDB entries from 2024-07-24

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