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3ZMC

Native structure of Farnesyl Pyrophosphate Synthase from Pseudomonas aeruginosa PA01, with bound substrate molecule Geranyl pyrophosphate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0004659molecular_functionprenyltransferase activity
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GPP A 1295
ChainResidue
ASER79
AHOH2084
AHOH2091
AHOH2092
AHOH2215
AHOH2216
AHOH2218
AASP83
AASP89
AARG94
AVAL154
AGLN157
ALYS180
AMG1296
AMG1297

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1296
ChainResidue
AASP83
AASP89
AGPP1295
AMG1297
AHOH2084
AHOH2092

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1297
ChainResidue
AASP83
AASP89
AGPP1295
AMG1296
AHOH2082
AHOH2083
AHOH2091

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 1298
ChainResidue
AGLN221
AVAL291
AGLU292
AARG293
AARG294

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GPP B 1292
ChainResidue
BSER79
BHIS82
BASP83
BASP89
BARG94
BGLN157
BLYS180
BMG1293
BMG1294
BHOH2087
BHOH2088
BHOH2092
BHOH2093
BHOH2194
BHOH2195
BHOH2196

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1293
ChainResidue
BASP83
BASP89
BGPP1292
BMG1294
BHOH2088
BHOH2093

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1294
ChainResidue
BASP83
BASP89
BGPP1292
BMG1293
BHOH2086
BHOH2087
BHOH2092

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1295
ChainResidue
BASP223
BHOH2137
BHOH2164
BHOH2167
BHOH2168
BHOH2197

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1296
ChainResidue
BTYR5
BARG8
BARG12
BGLU56
BHOH2198

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQVqDDIlD
ChainResidueDetails
AILE214-ASP226

site_idPS00723
Number of Residues17
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVhDDlpamDdddlRRG
ChainResidueDetails
ALEU80-GLY96

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PDB entries from 2024-06-05

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