Structure of PDB 1dce Chain D

Receptor sequence
>1dceD (length=329) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TQQKDVTIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYW
GLTVMDLMGQLHRMNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAV
QILTLYDSIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVAT
LALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLA
ITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKII
GRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLG
EEQIKPVSPVFCMPEEVLQRVNVQPELVS
3D structure
PDB1dce Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) H188 R230 K233 D236 C238 Y239 D278 D285 H288
Enzyme Commision number 2.5.1.60: protein geranylgeranyltransferase type II.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN D D238 C240 H290 D236 C238 H288
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:1dce, PDBe:1dce, PDBj:1dce
PDBsum1dce
PubMed10745007
UniProtQ08603|PGTB2_RAT Geranylgeranyl transferase type-2 subunit beta (Gene Name=Rabggtb)

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