Structure of PDB 1ltx Chain B Binding Site BS01
Receptor Information
>1ltx Chain B (length=318) Species:
10116
(Rattus norvegicus) [
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KDVTIKSDPDTLLLEKHADYIASYGSCMSEYLRMSGVYWGLTVMDLMGQL
HRMNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAVQILTLYDSIHV
INVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAIN
VEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSD
LLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKL
RSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVF
CMPEEVLQRVNVQPELVS
Ligand information
>1ltx Chain P (length=4) [
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AAAA
Receptor-Ligand Complex Structure
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PDB
1ltx
Structure of Rab Escort Protein-1 in Complex with Rab Geranylgeranyltransferase
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
H190 Y241 D287 F289
Binding residue
(residue number reindexed from 1)
H177 Y228 D274 F276
Enzymatic activity
Catalytic site (original residue number in PDB)
H190 R232 K235 D238 C240 Y241 D280 D287 H290
Catalytic site (residue number reindexed from 1)
H177 R219 K222 D225 C227 Y228 D267 D274 H277
Enzyme Commision number
2.5.1.60
: protein geranylgeranyltransferase type II.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004659
prenyltransferase activity
GO:0004661
protein geranylgeranyltransferase activity
GO:0004663
Rab geranylgeranyltransferase activity
GO:0005515
protein binding
GO:0008270
zinc ion binding
GO:0008318
protein prenyltransferase activity
GO:0019840
isoprenoid binding
GO:0031267
small GTPase binding
GO:0046872
metal ion binding
Biological Process
GO:0018344
protein geranylgeranylation
Cellular Component
GO:0005968
Rab-protein geranylgeranyltransferase complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1ltx
,
PDBe:1ltx
,
PDBj:1ltx
PDBsum
1ltx
PubMed
12620235
UniProt
Q08603
|PGTB2_RAT Geranylgeranyl transferase type-2 subunit beta (Gene Name=Rabggtb)
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