eF-site ID 1mwn_16-ABXY
PDB Code 1mwn
Model 16
Chain A, B, X, Y

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Title Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12
Classification STRUCTURAL PROTEIN
Compound S-100 protein, beta chain
Source Rattus norvegicus (Rat) (CAZA1_HUMAN)
Sequence A:  SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNEL
SHFLEEIKEQEVVDKVMETLDEDGDGECDFQEFMAFVSMV
TTACHEFFEHE
B:  SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNEL
SHFLEEIKEQEVVDKVMETLDEDGDGECDFQEFMAFVSMV
TTACHEFFEHE
X:  TRTKIDWNKILS
Y:  TRTKIDWNKILS
Description


Functional site

1) chain A
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

2) chain A
residue 23
type
sequence D
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

3) chain A
residue 24
type
sequence K
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

4) chain A
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

5) chain A
residue 27
type
sequence L
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

6) chain A
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE CA A 100
source : AC1

7) chain A
residue 61
type
sequence D
description BINDING SITE FOR RESIDUE CA A 101
source : AC2

8) chain A
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE CA A 101
source : AC2

9) chain A
residue 65
type
sequence D
description BINDING SITE FOR RESIDUE CA A 101
source : AC2

10) chain A
residue 67
type
sequence E
description BINDING SITE FOR RESIDUE CA A 101
source : AC2

11) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CA A 101
source : AC2

12) chain B
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

13) chain B
residue 23
type
sequence D
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

14) chain B
residue 24
type
sequence K
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

15) chain B
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

16) chain B
residue 27
type
sequence L
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

17) chain B
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE CA B 102
source : AC3

18) chain B
residue 61
type
sequence D
description BINDING SITE FOR RESIDUE CA B 103
source : AC4

19) chain B
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE CA B 103
source : AC4

20) chain B
residue 65
type
sequence D
description BINDING SITE FOR RESIDUE CA B 103
source : AC4

21) chain B
residue 67
type
sequence E
description BINDING SITE FOR RESIDUE CA B 103
source : AC4

22) chain B
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CA B 103
source : AC4

23) chain A
residue 2
type MOD_RES
sequence E
description N-acetylserine => ECO:0000250|UniProtKB:P02638
source Swiss-Prot : SWS_FT_FI4

24) chain B
residue 2
type MOD_RES
sequence E
description N-acetylserine => ECO:0000250|UniProtKB:P02638
source Swiss-Prot : SWS_FT_FI4

25) chain A
residue 61-73
type prosite
sequence DEDGDGECDFQEF
description EF_HAND_1 EF-hand calcium-binding domain. DEDGDGECDfqEF
source prosite : PS00018

26) chain A
residue 56-77
type prosite
sequence VMETLDEDGDGECDFQEFMAFV
description S100_CABP S-100/ICaBP type calcium binding protein signature. VMetLDedgDgecDFqEFmaFV
source prosite : PS00303

27) chain A
residue 62
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

28) chain B
residue 73
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 64
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 66
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 68
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 73
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 62
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 64
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

35) chain B
residue 66
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 68
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 16
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 26
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 86
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 91
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 16
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 26
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 86
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 91
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:14621986
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 19
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 22
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 27
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 19
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 22
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 27
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18949447, ECO:0007744|PDB:2K7O
source Swiss-Prot : SWS_FT_FI2


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