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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
A0008270molecular_functionzinc ion binding
A0008318molecular_functionprotein prenyltransferase 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
B0005968cellular_componentRab-protein geranylgeranyltransferase complex
B0008270molecular_functionzinc ion binding
B0008318molecular_functionprotein prenyltransferase 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
R0005737cellular_componentcytoplasm
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 Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18756270, ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSX
ChainResidueDetails
BHIS190

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166
ChainResidueDetails
BASP238
BCYS240
BHIS290

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSV
ChainResidueDetails
BTYR241

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000250|UniProtKB:P53611
ChainResidueDetails
BGLY2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P53611
ChainResidueDetails
BTHR3

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

226707

PDB entries from 2024-10-30

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