eF-site ID 2cls-AB
PDB Code 2cls
Chain A, B

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Title The crystal structure of the human RND1 GTPase in the active GTP bound state
Classification NUCLEOTIDE BINDING PROTEIN
Compound RHO-RELATED GTP-BINDING PROTEIN RHO6
Source Homo sapiens (Human) (RND1_HUMAN)
Sequence A:  VVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFEN
YTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVL
LCFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDL
RTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSA
FTSEKSIHSIFRTASMLCL
B:  VARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENY
TACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLL
CFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDLR
TDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAF
TSEKSIHSIFRTASMLCL
Description


Functional site

1) chain A
residue 27
type
sequence T
description BINDING SITE FOR RESIDUE MG A 550
source : AC1

2) chain A
residue 45
type
sequence T
description BINDING SITE FOR RESIDUE MG A 550
source : AC1

3) chain B
residue 27
type
sequence T
description BINDING SITE FOR RESIDUE MG B 550
source : AC2

4) chain B
residue 45
type
sequence T
description BINDING SITE FOR RESIDUE MG B 550
source : AC2

5) chain A
residue 22
type
sequence V
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

6) chain A
residue 23
type
sequence Q
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

7) chain A
residue 24
type
sequence C
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

8) chain A
residue 25
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

9) chain A
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

10) chain A
residue 27
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

11) chain A
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

12) chain A
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

13) chain A
residue 39
type
sequence P
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

14) chain A
residue 40
type
sequence E
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

15) chain A
residue 41
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

16) chain A
residue 42
type
sequence Y
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

17) chain A
residue 45
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

18) chain A
residue 69
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

19) chain A
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

20) chain A
residue 126
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

21) chain A
residue 128
type
sequence D
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

22) chain A
residue 129
type
sequence L
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

23) chain A
residue 168
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

24) chain A
residue 169
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

25) chain A
residue 170
type
sequence F
description BINDING SITE FOR RESIDUE GTP A 500
source : AC3

26) chain B
residue 22
type
sequence V
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

27) chain B
residue 23
type
sequence Q
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

28) chain B
residue 24
type
sequence C
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

29) chain B
residue 25
type
sequence G
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

30) chain B
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

31) chain B
residue 27
type
sequence T
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

32) chain B
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

33) chain B
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

34) chain B
residue 39
type
sequence P
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

35) chain B
residue 40
type
sequence E
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

36) chain B
residue 41
type
sequence T
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

37) chain B
residue 42
type
sequence Y
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

38) chain B
residue 45
type
sequence T
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

39) chain B
residue 69
type
sequence S
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

40) chain B
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

41) chain B
residue 126
type
sequence K
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

42) chain B
residue 128
type
sequence D
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

43) chain B
residue 129
type
sequence L
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

44) chain B
residue 168
type
sequence S
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

45) chain B
residue 169
type
sequence A
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

46) chain B
residue 170
type
sequence F
description BINDING SITE FOR RESIDUE GTP B 500
source : AC4

47) chain A
residue 23
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

48) chain B
residue 169
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

49) chain A
residue 38
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 67
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

51) chain A
residue 125
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

52) chain A
residue 169
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 23
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 38
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 67
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1

56) chain B
residue 125
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:19843518, ECO:0007744|PDB:2CLS
source Swiss-Prot : SWS_FT_FI1


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