Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TS7

CRYSTAL STRUCTURE OF FARNESYL DIPHOSPHATE SYNTHASE (TARGET EFI-501951) FROM Methylococcus capsulatus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
A0008654biological_processphospholipid biosynthetic process
A0016114biological_processterpenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0045337biological_processfarnesyl diphosphate biosynthetic process
A0046872molecular_functionmetal ion binding
B0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
B0004659molecular_functionprenyltransferase activity
B0005737cellular_componentcytoplasm
B0008299biological_processisoprenoid biosynthetic process
B0008654biological_processphospholipid biosynthetic process
B0016114biological_processterpenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0045337biological_processfarnesyl diphosphate biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 323
ChainResidue
ALYS49
AMET51
AARG52
AHIS81
APO4324
AHOH325

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 324
ChainResidue
AARG100
APO4323
AHOH325
AHOH339
AGLY48
ALYS49
AHIS81

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 323
ChainResidue
BLYS49
BMET51
BARG52
BHIS81
BARG298
BPO4324
BHOH328

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 324
ChainResidue
BGLY48
BLYS49
BHIS81
BLEU85
BPO4323
BHOH326
BHOH328

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 325
ChainResidue
BILE63
BARG201
BLEU204
BGLN208
BPHE281

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQIqDDIlD
ChainResidueDetails
AILE219-ASP231

site_idPS00723
Number of Residues17
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDdddlRRG
ChainResidueDetails
ALEU85-GLY101

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon