eF-site ID 6dha-AB
PDB Code 6dha
Chain A, B

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Title Crystal Structure of Human PPARgamma Ligand Binding Domain in Complex with Hydroxy Pioglitazone (M-IV)
Classification transcription/transcription inhibitor
Compound Peroxisome proliferator-activated receptor gamma
Source (PPARG_HUMAN)
Sequence A:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP
FVIYDMNSLMMGEDEVAIRIFQGCQFRSVEAVQEITEYAK
SIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLI
SEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDD
SDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQL
KLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTET
DMSLHPLLQEIYKDL
B:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP
FVIYDMNSLMMGEDKIKFKHITEVAIRIFQGCQFRSVEAV
QEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASL
MNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVK
FNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNL
LQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLL
QVIKKTETDMSLHPLLQEIYKDL
Description


Functional site

1) chain A
residue 281
type
sequence I
description binding site for residue GFV A 501
source : AC1

2) chain A
residue 282
type
sequence F
description binding site for residue GFV A 501
source : AC1

3) chain A
residue 284
type
sequence G
description binding site for residue GFV A 501
source : AC1

4) chain A
residue 285
type
sequence C
description binding site for residue GFV A 501
source : AC1

5) chain A
residue 286
type
sequence Q
description binding site for residue GFV A 501
source : AC1

6) chain A
residue 289
type
sequence S
description binding site for residue GFV A 501
source : AC1

7) chain A
residue 323
type
sequence H
description binding site for residue GFV A 501
source : AC1

8) chain A
residue 327
type
sequence Y
description binding site for residue GFV A 501
source : AC1

9) chain A
residue 330
type
sequence L
description binding site for residue GFV A 501
source : AC1

10) chain A
residue 341
type
sequence I
description binding site for residue GFV A 501
source : AC1

11) chain A
residue 364
type
sequence M
description binding site for residue GFV A 501
source : AC1

12) chain A
residue 449
type
sequence H
description binding site for residue GFV A 501
source : AC1

13) chain A
residue 473
type
sequence Y
description binding site for residue GFV A 501
source : AC1

14) chain A
residue 228
type
sequence L
description binding site for residue KNA A 502
source : AC2

15) chain A
residue 288
type
sequence R
description binding site for residue KNA A 502
source : AC2

16) chain A
residue 329
type
sequence M
description binding site for residue KNA A 502
source : AC2

17) chain A
residue 330
type
sequence L
description binding site for residue KNA A 502
source : AC2

18) chain A
residue 333
type
sequence L
description binding site for residue KNA A 502
source : AC2

19) chain A
residue 342
type
sequence S
description binding site for residue KNA A 502
source : AC2

20) chain A
residue 343
type
sequence E
description binding site for residue KNA A 502
source : AC2

21) chain A
residue 258
type
sequence G
description binding site for residue KNA A 503
source : AC3

22) chain B
residue 249
type
sequence I
description binding site for residue GFV B 501
source : AC4

23) chain B
residue 255
type
sequence L
description binding site for residue GFV B 501
source : AC4

24) chain B
residue 259
type
sequence E
description binding site for residue GFV B 501
source : AC4

25) chain B
residue 264
type
sequence F
description binding site for residue GFV B 501
source : AC4

26) chain B
residue 266
type
sequence H
description binding site for residue GFV B 501
source : AC4

27) chain B
residue 267
type
sequence I
description binding site for residue GFV B 501
source : AC4

28) chain B
residue 280
type
sequence R
description binding site for residue GFV B 501
source : AC4

29) chain B
residue 281
type
sequence I
description binding site for residue GFV B 501
source : AC4

30) chain B
residue 285
type
sequence C
description binding site for residue GFV B 501
source : AC4

31) chain B
residue 288
type
sequence R
description binding site for residue GFV B 501
source : AC4

32) chain B
residue 292
type
sequence A
description binding site for residue GFV B 501
source : AC4

33) chain B
residue 326
type
sequence I
description binding site for residue GFV B 501
source : AC4

34) chain B
residue 330
type
sequence L
description binding site for residue GFV B 501
source : AC4

35) chain B
residue 341
type
sequence I
description binding site for residue GFV B 501
source : AC4

36) chain B
residue 348
type
sequence M
description binding site for residue GFV B 501
source : AC4

37) chain A
residue 286
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 323
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 449
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 473
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 286
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 323
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 449
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 473
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 224
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 224
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649
source Swiss-Prot : SWS_FT_FI2


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