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1DCE

CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN

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
C0004659molecular_functionprenyltransferase activity
C0004661molecular_functionprotein geranylgeranyltransferase activity
C0004663molecular_functionRab geranylgeranyltransferase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005968cellular_componentRab-protein geranylgeranyltransferase complex
C0008270molecular_functionzinc ion binding
C0008318molecular_functionprotein prenyltransferase activity
C0018342biological_processprotein prenylation
C0018344biological_processprotein geranylgeranylation
C0031267molecular_functionsmall GTPase binding
D0003824molecular_functioncatalytic activity
D0004659molecular_functionprenyltransferase activity
D0004661molecular_functionprotein geranylgeranyltransferase activity
D0004663molecular_functionRab geranylgeranyltransferase activity
D0005515molecular_functionprotein binding
D0005968cellular_componentRab-protein geranylgeranyltransferase complex
D0008270molecular_functionzinc ion binding
D0008318molecular_functionprotein prenyltransferase activity
D0018344biological_processprotein geranylgeranylation
D0019840molecular_functionisoprenoid binding
D0031267molecular_functionsmall GTPase binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 900
ChainResidue
AHIS2
BASP238
BCYS240
BHIS290

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 950
ChainResidue
CHIS2
DASP238
DCYS240
DHIS290

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18756270, ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSX
ChainResidueDetails
BHIS190
DHIS190

site_idSWS_FT_FI2
Number of Residues6
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
DASP238
DCYS240
DHIS290

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSV
ChainResidueDetails
BTYR241
DTYR241

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000250|UniProtKB:P53611
ChainResidueDetails
BGLY2
DGLY2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P53611
ChainResidueDetails
BTHR3
DTHR3

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

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
CLYS105
DTYR241

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
CSER176

222415

PDB entries from 2024-07-10

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