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2Z50

S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with BPH-28

Functional Information from GO Data
ChainGOidnamespacecontents
A0004161molecular_functiondimethylallyltranstransferase activity
A0004311molecular_functionfarnesyltranstransferase activity
A0004337molecular_functiongeranyltranstransferase 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
B0004161molecular_functiondimethylallyltranstransferase activity
B0004311molecular_functionfarnesyltranstransferase activity
B0004337molecular_functiongeranyltranstransferase 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 Residues10
DetailsBINDING SITE FOR RESIDUE 028 A 1201
ChainResidue
AASP80
AHOH1314
AASP84
AARG89
AGLN147
ALYS174
AGLN211
AASP214
ALYS238
AHOH1240

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 028 B 1202
ChainResidue
BASP80
BASP84
BARG89
BGLN147
BLYS174
BGLN211
BASP214
BLYS238

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 Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:17535895
ChainResidueDetails
ALYS41
ALYS238
BLYS41
BARG44
BHIS73
BARG89
BARG90
BLYS174
BTHR175
BGLN211
BASN218
AARG44
BLYS238
AHIS73
AARG89
AARG90
ALYS174
ATHR175
AGLN211
AASN218

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895
ChainResidueDetails
AASP80
AASP84
BASP80
BASP84

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17535895
ChainResidueDetails
ALYS228
BLYS228

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for determining product chain length
ChainResidueDetails
ATYR112
BTYR112

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

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PDB entries from 2024-10-30

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