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6SXL

Crystal structure of CrtE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004161molecular_functiondimethylallyltranstransferase activity
A0004311molecular_functiongeranylgeranyl diphosphate synthase activity
A0004337molecular_function(2E,6E)-farnesyl diphosphate synthase activity
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
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
B0004659molecular_functionprenyltransferase activity
B0008299biological_processisoprenoid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue PO4 A 401
ChainResidue
AGLY52
ALYS53

site_idAC2
Number of Residues1
Detailsbinding site for residue PO4 B 401
ChainResidue
BHIS85

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQIvDDIlD
ChainResidueDetails
AILE221-ASP233
BILE221-ASP233

site_idPS00723
Number of Residues17
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDnddlRRG
ChainResidueDetails
ALEU89-GLY105
BLEU89-GLY105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14324","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Plays an important role in controlling prenyl chain elongation","evidences":[{"source":"PubMed","id":"32523588","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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