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3DSX

Crystal structure of RabGGTase(DELTA LRR; DELTA IG)in complex with di-prenylated peptide Ser-Cys(GG)-Ser-Cys(GG) derivated from Rab7

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 332
ChainResidue
AHIS2
BASP238
BCYS240
BHIS290
BGER334

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 333
ChainResidue
BHOH406
AALA138
BHIS64
BMET66
BHOH405

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GER B 334
ChainResidue
AHIS2
BLEU96
BGLN103
BGLY192
BCYS196
BCYS240
BTYR241
BTRP244
BZN332

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 Residues1
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
BTYR241

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
ALYS105

221716

PDB entries from 2024-06-26

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