Structure of PDB 1tn6 Chain B

Receptor sequence

>1tn6B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence]

SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE

3D structure

PDB

1tn6 Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity

Chain

Resolution

1.8 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)	H234 R277 K280 D283 C285 Y286 D338 D345 H348
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)
BS01	peptide	B	Y581 Y593 C595 S599 W602 A651 P652 R702 S857 R858 Y861 H862	Y67 Y79 C81 S85 W88 A137 P138 R188 S343 R344 Y347 H348
BS02	GLC	B	Q733 N734 W735	Q219 N220 W221
BS03	FRU	B	Q733 N734 N769 S772	Q219 N220 N255 S258
BS04	FII	B	Y705 H748 G750 Y751 C754 R791 K794 Y800 W803	Y191 H234 G236 Y237 C240 R277 K280 Y286 W289
BS05	ZN	B	D797 C799 H862	D283 C285 H348

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

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