eF-site ID 1xvp-ABCDEFGH
PDB Code 1xvp
Chain A, B, C, D, E, F, G, H

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Title crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid and CITCO
Classification DNA BINDING PROTEIN
Compound Retinoic acid receptor RXR-alpha
Source Homo sapiens (Human) (NP_003734)
Sequence A:  NEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVT
NICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWN
ELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIF
DRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNP
AEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALR
SIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAP
B:  PVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLF
IHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVF
RSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPL
RYTIEDGARVGFQVEFLELLFHFHGTLRKLQLQEPEYVLL
AAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRR
PRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPL
LQEICS
C:  NEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVT
NICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWN
ELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIF
DRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNP
AEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALR
SIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
D:  PVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLF
IHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVF
RSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPL
RYTIEDGARVGFQVEFLELLFHFHGTLRKLQLQEPEYVLL
AAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRR
PRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPL
LQEICS
E:  HKILHRLLQE
F:  RHKILHRLLQEG
G:  ERHKILHRLLQE
H:  ERHKILHRLLQE
Description


Functional site

1) chain C
residue 268
type
sequence I
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

2) chain C
residue 272
type
sequence A
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

3) chain C
residue 275
type
sequence Q
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

4) chain C
residue 313
type
sequence F
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

5) chain C
residue 316
type
sequence R
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

6) chain C
residue 326
type
sequence L
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

7) chain C
residue 327
type
sequence A
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

8) chain C
residue 345
type
sequence I
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

9) chain C
residue 432
type
sequence C
description BINDING SITE FOR RESIDUE F15 C 1001
source : AC1

10) chain A
residue 272
type
sequence A
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

11) chain A
residue 275
type
sequence Q
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

12) chain A
residue 313
type
sequence F
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

13) chain A
residue 316
type
sequence R
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

14) chain A
residue 327
type
sequence A
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

15) chain A
residue 345
type
sequence I
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

16) chain A
residue 432
type
sequence C
description BINDING SITE FOR RESIDUE F15 A 1002
source : AC2

17) chain D
residue 161
type
sequence F
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

18) chain D
residue 165
type
sequence N
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

19) chain D
residue 168
type
sequence M
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

20) chain D
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

21) chain D
residue 203
type
sequence H
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

22) chain D
residue 206
type
sequence L
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

23) chain D
residue 217
type
sequence F
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

24) chain D
residue 224
type
sequence Y
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

25) chain D
residue 225
type
sequence T
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

26) chain D
residue 228
type
sequence D
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

27) chain D
residue 229
type
sequence G
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

28) chain D
residue 239
type
sequence L
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

29) chain D
residue 242
type
sequence L
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

30) chain D
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

31) chain D
residue 326
type
sequence Y
description BINDING SITE FOR RESIDUE CID D 1003
source : AC3

32) chain A
residue 316
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 327
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6
source Swiss-Prot : SWS_FT_FI1

34) chain C
residue 316
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6
source Swiss-Prot : SWS_FT_FI1

35) chain C
residue 327
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6
source Swiss-Prot : SWS_FT_FI1

36) chain A
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI2

37) chain C
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 260
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700
source Swiss-Prot : SWS_FT_FI3

39) chain C
residue 260
type MOD_RES
sequence S
description Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700
source Swiss-Prot : SWS_FT_FI3


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