eF-site ID 1nl4-AB
PDB Code 1nl4
Chain A, B

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Title Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor
Classification TRANSFERASE
Compound Protein farnesyltransferase alpha subunit
Source Rattus norvegicus (Rat) (PFTB_RAT)
Sequence A:  FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSE
KFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVW
HFRRVLLRSLQKDLQEEMNYITAIIEEQPKNYQVWHHRRV
LVEWLKDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFR
LWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPN
LLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDIL
NKALELCEILAKEKDTIRKEYWRYIGRSLQSK
B:  LYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSY
KFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPW
LCYWILHSLELLDEPIPQIVATDVCQFLELCQSPDGGFGG
GPGQYPHLAPTYAAVNALCIIGTEEAYNVINREKLLQYLY
SLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLF
EGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVIL
KKERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSF
WQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMC
CQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAML
HDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVPG
F
Description


Functional site

1) chain B
residue 297
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 500
source : AC1

2) chain B
residue 299
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 500
source : AC1

3) chain B
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 500
source : AC1

4) chain A
residue 164
type
sequence K
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

5) chain A
residue 166
type
sequence Y
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

6) chain B
residue 102
type
sequence W
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

7) chain B
residue 205
type
sequence Y
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

8) chain B
residue 248
type
sequence H
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

9) chain B
residue 251
type
sequence Y
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

10) chain B
residue 291
type
sequence R
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

11) chain B
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

12) chain B
residue 303
type
sequence W
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

13) chain B
residue 361
type
sequence Y
description BINDING SITE FOR RESIDUE HFP B 501
source : AC2

14) chain A
residue 166
type
sequence Y
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

15) chain B
residue 102
type
sequence W
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

16) chain B
residue 106
type
sequence W
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

17) chain B
residue 297
type
sequence D
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

18) chain B
residue 352
type
sequence D
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

19) chain B
residue 359
type
sequence D
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

20) chain B
residue 360
type
sequence F
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

21) chain B
residue 361
type
sequence Y
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

22) chain B
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE FTL B 1
source : AC3

23) chain B
residue 248
type catalytic
sequence H
description 484
source MCSA : MCSA1

24) chain B
residue 291
type catalytic
sequence R
description 484
source MCSA : MCSA1

25) chain B
residue 294
type catalytic
sequence K
description 484
source MCSA : MCSA1

26) chain B
residue 297
type catalytic
sequence D
description 484
source MCSA : MCSA1

27) chain B
residue 299
type catalytic
sequence C
description 484
source MCSA : MCSA1

28) chain B
residue 300
type catalytic
sequence Y
description 484
source MCSA : MCSA1

29) chain B
residue 352
type catalytic
sequence D
description 484
source MCSA : MCSA1

30) chain B
residue 359
type catalytic
sequence D
description 484
source MCSA : MCSA1

31) chain B
residue 362
type catalytic
sequence H
description 484
source MCSA : MCSA1

32) chain B
residue 248
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 291
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 300
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 297
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 299
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 362
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 102
type SITE
sequence W
description Important for selectivity against geranylgeranyl diphosphate => ECO:0000250|UniProtKB:P49356
source Swiss-Prot : SWS_FT_FI3


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