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4RXA

Crystal structure of human farnesyl diphosphate synthase in complex with BPH-1358

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 Residues14
DetailsBINDING SITE FOR RESIDUE 3F2 A 1001
ChainResidue
ALYS14
AVAL340
AGLY343
ALEU344
ALYS347
APO41002
ALYS57
AASN59
AARG60
ALEU62
ATHR63
AVAL66
APHE239
AASP243

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1002
ChainResidue
AGLY56
ALYS57
AGLN96
AARG113
A3F21001
AHOH2037
AHOH2070
AHOH2071

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
ATHR201
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 2024-07-17

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