BioLiP

Receptor Information

>1jcq Chain B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE

Ligand ID

739

InChI

InChI=1S/C23H39N3O6S2/c1-4-16(2)20(25-13-18(24)15-33)14-32-21(12-17-8-6-5-7-9-17)22(27)26-19(23(28)29)10-11-34(3,30)31/h5-9,16,18-21,25,33H,4,10-15,24H2,1-3H3,(H,26,27)(H,28,29)/t16-,18+,19-,20+,21-/m0/s1

InChIKey

SIEXHGZWGJLLAC-OSTWSGHESA-N

SMILES

Software	SMILES
CACTVS 3.341	CC[CH](C)[CH](CO[CH](Cc1ccccc1)C(=O)N[CH](CC[S](C)(=O)=O)C(O)=O)NC[CH](N)CS
OpenEye OEToolkits 1.5.0	CC[C@H](C)[C@@H](CO[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCS(=O)(=O)C)C(=O)O)NC[C@H](CS)N
OpenEye OEToolkits 1.5.0	CCC(C)C(COC(Cc1ccccc1)C(=O)NC(CCS(=O)(=O)C)C(=O)O)NCC(CS)N
CACTVS 3.341	CC[C@H](C)[C@@H](CO[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC[S](C)(=O)=O)C(O)=O)NC[C@@H](N)CS
ACDLabs 10.04	O=S(=O)(C)CCC(C(=O)O)NC(=O)C(OCC(NCC(N)CS)C(C)CC)Cc1ccccc1

Formula

C23 H39 N3 O6 S2

Name

2(S)-{2(S)-[2(R)-AMINO-3-MERCAPTO]PROPYLAMINO-3(S)-METHYL}PENTYLOXY-3-PHENYLPROPIONYLMETHIONINE SULFONE;
L-739,750

PDB chain

1jcq Chain B Residue 3012 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1jcq The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Resolution	2.3 Å
Binding residue (original residue number in PDB)	S99 W102 W106 P152 R202 D297 C299 Y300 H362
Binding residue (residue number reindexed from 1)	S85 W88 W92 P138 R188 D283 C285 Y286 H348
Annotation score	1

Catalytic site (original residue number in PDB)	H248 R291 K294 D297 C299 Y300 D352 D359 H362
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.

	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

PDB	RCSB:1jcq, PDBe:1jcq, PDBj:1jcq
PDBsum	1jcq
PubMed	11687658
UniProt	P49356\|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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Structure of PDB 1jcq Chain B Binding Site BS05