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3PZ2

Crystal structure of RabGGTase(DELTA LRR; DELTA IG) in Complex with BMS3 and lipid substrate GGPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0008318molecular_functionprotein prenyltransferase activity
A0018342biological_processprotein prenylation
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BASP238
BCYS240
BHIS290
B3PZ333

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 332
ChainResidue
AALA138
AHOH355
BHIS64
BMET66

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3PZ B 333
ChainResidue
BTYR44
BLEU45
BASP238
BASP287
BPRO288
BPHE289
BHIS290
BGRG334
BHOH375
BZN1

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GRG B 334
ChainResidue
ALYS105
APHE143
AHOH344
BTYR51
BLEU96
BGLN103
BARG144
BPHE147
BHIS190
BGLY192
BGLN193
BTYR195
BCYS196
BARG232
BLYS235
BCYS240
BTYR241
BPHE293
B3PZ333
BHOH346
BHOH352
BHOH375
BHOH392
BHOH396
BHOH397

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

site_idSWS_FT_FI5
Number of Residues41
DetailsRepeat: {"description":"PFTB 2"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"PFTB 3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues41
DetailsRepeat: {"description":"PFTB 4"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues41
DetailsRepeat: {"description":"PFTB 5"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsRepeat: {"description":"PFTB 6"}
ChainResidueDetails

site_idSWS_FT_FI10
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_FI11
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_FI12
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3DST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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