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2E91

S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-91

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004161molecular_functiondimethylallyltranstransferase activity
A0004311molecular_functiongeranylgeranyl diphosphate synthase activity
A0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0008299biological_processisoprenoid biosynthetic process
A0015031biological_processprotein transport
A0016114biological_processterpenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0033384biological_processgeranyl diphosphate biosynthetic process
A0033386biological_processgeranylgeranyl diphosphate biosynthetic process
A0045337biological_processfarnesyl diphosphate biosynthetic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004161molecular_functiondimethylallyltranstransferase activity
B0004311molecular_functiongeranylgeranyl diphosphate synthase activity
B0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
B0004659molecular_functionprenyltransferase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0008299biological_processisoprenoid biosynthetic process
B0015031biological_processprotein transport
B0016114biological_processterpenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0033384biological_processgeranyl diphosphate biosynthetic process
B0033386biological_processgeranylgeranyl diphosphate biosynthetic process
B0045337biological_processfarnesyl diphosphate biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1301
ChainResidue
AASP80
AASP84
AHOH636
AHOH637
AHOH638
AZOL901
AMG1302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1302
ChainResidue
AHOH634
AHOH635
AZOL901
AMG1301
AASP80
AASP84

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1303
ChainResidue
BASP80
BASP84
BHOH646
BZOL902
BMG1304

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1304
ChainResidue
BASP80
BASP84
BHOH647
BHOH648
BHOH649
BZOL902
BMG1303

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ZOL A 901
ChainResidue
AASP80
AASP84
AARG89
AGLN147
ALYS174
ATHR175
AGLN211
AASP214
ALYS238
AHOH481
AHOH570
AHOH635
AHOH636
AHOH639
AHOH640
AMG1301
AMG1302

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ZOL B 902
ChainResidue
BASP80
BASP84
BARG89
BGLN147
BLYS174
BTHR175
BGLN211
BASP214
BLYS238
BHOH646
BHOH648
BHOH651
BMG1303
BMG1304

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGiiYQIrDDYlN
ChainResidueDetails
ALEU206-ASN218

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnaplRRG
ChainResidueDetails
ALEU77-GLY91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17535895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16554305","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17535895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for determining product chain length"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fps
ChainResidueDetails
ATYR210
AARG89

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fps
ChainResidueDetails
BTYR210
BARG89

238895

PDB entries from 2025-07-16

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