Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2F8Z

Crystal structure of human FPPS in complex with zoledronate and isopentenyl diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
F0008299biological_processisoprenoid biosynthetic process
F0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 1001
ChainResidue
FASP103
FASP107
FMG1003
FZOL5001
FHOH9018
FHOH9022

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 1002
ChainResidue
FHOH9007
FHOH9009
FASP243
FZOL5001
FHOH9005

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG F 1003
ChainResidue
FASP103
FASP107
FMG1001
FZOL5001
FHOH9002
FHOH9003
FHOH9004

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IPE F 9001
ChainResidue
FGLY56
FLYS57
FARG60
FGLN96
FARG113
FTHR201
FPHE239
FGLN240
FASP243
FZOL5001
FHOH9017
FHOH9062

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ZOL F 5001
ChainResidue
FASP103
FASP107
FARG112
FLYS200
FTHR201
FGLN240
FASP243
FLYS257
FMG1001
FMG1002
FMG1003
FIPE9001
FHOH9005
FHOH9006
FHOH9007
FHOH9009
FHOH9013
FHOH9018
FHOH9022

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
FGLY123
FLEU126
FGLN162
FILE169
FLEU173
FPRO179

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
FALA178
FLYS266
FCYS267
FGLU306
FSER323

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
FTYR332

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for determining product chain length => ECO:0000250
ChainResidueDetails
FSER164
FTYR165

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
FGLY123

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
FLYS353

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon