Structure of PDB 1tn6 Chain B Binding Site BS01

Receptor Information

>1tn6 Chain B (length=410) Species: 9606 (Homo sapiens)

SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE

Ligand information

>1tn6 Chain C (length=11)

DDPTASACNIQ

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1tn6 Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): Y581 Y593 C595 S599 W602 A651 P652 R702 S857 R858 Y861 H862
• Binding residue (residue number reindexed from 1): Y67 Y79 C81 S85 W88 A137 P138 R188 S343 R344 Y347 H348

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): H234 R277 K280 D283 C285 Y286 D338 D345 H348
• Enzyme Commision number: 2.5.1.58: protein farnesyltransferase.

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

External links

• PDB: RCSB:1tn6, PDBe:1tn6, PDBj:1tn6
• PDBsum: 1tn6
• PubMed: 15451670
• UniProt: P49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)