Structure of PDB 1ld7 Chain B

Receptor sequence
>1ld7B (length=407) Species: 9606 (Homo sapiens) [Search protein sequence]
PVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNH
LVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDE
PIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTE
EAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNI
ITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRER
SLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALH
AQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYC
LSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFL
QKPVPGF
3D structure
PDB1ld7 3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency.
ChainB
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) H748 R791 K794 D797 C799 Y800 D852 D859 H862
Catalytic site (residue number reindexed from 1) H232 R275 K278 D281 C283 Y284 D336 D343 H346
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
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 GLC B Q733 N734 W735 Q217 N218 W219
BS02 FRU B Q733 N734 G737 N769 S772 Q217 N218 G221 N253 S256
BS03 ZN B D797 C799 H862 D281 C283 H346
BS04 FPP B H748 G750 Y751 R791 K794 Y800 W803 H232 G234 Y235 R275 K278 Y284 W287
BS05 U66 B S599 W602 W606 R702 D797 C799 Y861 H862 S83 W86 W90 R186 D281 C283 Y345 H346 MOAD: ic50=1.1nM
PDBbind-CN: -logKd/Ki=8.96,IC50=1.1nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0018343 protein farnesylation
Cellular Component
GO:0005829 cytosol
GO:0005875 microtubule associated complex
GO:0005965 protein farnesyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ld7, PDBe:1ld7, PDBj:1ld7
PDBsum1ld7
PubMed12036349
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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