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

1LTX

Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0004661molecular_functionprotein geranylgeranyltransferase activity
A0004663molecular_functionRab geranylgeranyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005968cellular_componentRab-protein geranylgeranyltransferase complex
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0008270molecular_functionzinc ion binding
A0008318molecular_functionprotein prenyltransferase activity
A0016740molecular_functiontransferase activity
A0018342biological_processprotein prenylation
A0018344biological_processprotein geranylgeranylation
A0031267molecular_functionsmall GTPase binding
B0003824molecular_functioncatalytic activity
B0004659molecular_functionprenyltransferase activity
B0004661molecular_functionprotein geranylgeranyltransferase activity
B0004663molecular_functionRab geranylgeranyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005968cellular_componentRab-protein geranylgeranyltransferase complex
B0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
B0008270molecular_functionzinc ion binding
B0008318molecular_functionprotein prenyltransferase activity
B0016740molecular_functiontransferase activity
B0018344biological_processprotein geranylgeranylation
B0019840molecular_functionisoprenoid binding
B0031267molecular_functionsmall GTPase binding
B0046872molecular_functionmetal ion binding
R0001568biological_processblood vessel development
R0005092molecular_functionGDP-dissociation inhibitor activity
R0005096molecular_functionGTPase activator activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005829cellular_componentcytosol
R0005968cellular_componentRab-protein geranylgeranyltransferase complex
R0006612biological_processprotein targeting to membrane
R0006886biological_processintracellular protein transport
R0007264biological_processsmall GTPase-mediated signal transduction
R0016192biological_processvesicle-mediated transport
R0018344biological_processprotein geranylgeranylation
R0031267molecular_functionsmall GTPase binding
R0044877molecular_functionprotein-containing complex binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 900
ChainResidue
BASP238
BCYS240
BHIS290

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL R 901
ChainResidue
RTYR234
RGLY580
RASN581
RHOH916

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FAR P 1428
ChainResidue
BGLN103
BARG144
BTYR195
PALA9
PALA11
PALA12
ATYR107
BTYR51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsRepeat: {"description":"PFTA 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues34
DetailsRepeat: {"description":"PFTA 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRepeat: {"description":"PFTA 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsRepeat: {"description":"PFTA 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues34
DetailsRepeat: {"description":"PFTA 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsRepeat: {"description":"PFTA 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9JHK4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues41
DetailsRepeat: {"description":"PFTB 2"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues41
DetailsRepeat: {"description":"PFTB 3"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues41
DetailsRepeat: {"description":"PFTB 4"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues41
DetailsRepeat: {"description":"PFTB 5"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues42
DetailsRepeat: {"description":"PFTB 6"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18756270","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18399557","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18756270","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19894725","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22480322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22963166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3DST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
ALYS105
BTYR241

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
ASER176

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon