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5JA0

Crystal structure of human FPPS with allosterically bound FPP

Functional Information from GO Data
ChainGOidnamespacecontents
F0004659molecular_functionprenyltransferase activity
F0008299biological_processisoprenoid biosynthetic process
F0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 F 401
ChainResidue
FGLY56
FLYS57
FGLN96
FARG113
FFPP402
FHOH528
FHOH529
FHOH537
FHOH569

site_idAC2
Number of Residues14
Detailsbinding site for residue FPP F 402
ChainResidue
FTYR10
FLYS57
FASN59
FARG60
FTHR63
FVAL66
FSER205
FPHE239
FVAL340
FLEU344
FLYS347
FPO4401
FHOH537
FHOH611

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD
ChainResidueDetails
FMET235-ASP247

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG
ChainResidueDetails
FLEU100-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
ChainResidueDetails
FLYS57
FARG60
FGLN96
FASP103
FASP107
FARG113

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
FARG112
FLYS200
FTHR201
FGLN240
FLYS257

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
FLYS266

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for determining product chain length => ECO:0000250
ChainResidueDetails
FPHE98
FPHE99

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
FLYS57

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
FLYS287

227111

PDB entries from 2024-11-06

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