eF-site ID 3hcm-AB
PDB Code 3hcm
Chain A, B

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Title Crystal structure of human S100B in complex with S45
Classification METAL BINDING PROTEIN
Compound Protein S100-B
Source Homo sapiens (Human) (S100B_HUMAN)
Sequence A:  MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNE
LSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAM
VTTACHEFFE
B:  MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNE
LSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAM
VTTACHEFFEH
Description


Functional site

1) chain A
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE CA A 92
source : AC1

2) chain A
residue 21
type
sequence E
description BINDING SITE FOR RESIDUE CA A 92
source : AC1

3) chain A
residue 23
type
sequence D
description BINDING SITE FOR RESIDUE CA A 92
source : AC1

4) chain A
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE CA A 92
source : AC1

5) chain A
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE CA A 92
source : AC1

6) chain A
residue 61
type
sequence D
description BINDING SITE FOR RESIDUE CA A 93
source : AC2

7) chain A
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE CA A 93
source : AC2

8) chain A
residue 65
type
sequence D
description BINDING SITE FOR RESIDUE CA A 93
source : AC2

9) chain A
residue 67
type
sequence E
description BINDING SITE FOR RESIDUE CA A 93
source : AC2

10) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CA A 93
source : AC2

11) chain A
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE S45 A 94
source : AC3

12) chain A
residue 60
type
sequence L
description BINDING SITE FOR RESIDUE S45 A 94
source : AC3

13) chain A
residue 76
type
sequence F
description BINDING SITE FOR RESIDUE S45 A 94
source : AC3

14) chain A
residue 79
type
sequence M
description BINDING SITE FOR RESIDUE S45 A 94
source : AC3

15) chain A
residue 45
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 95
source : AC4

16) chain B
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE CA B 92
source : AC5

17) chain B
residue 21
type
sequence E
description BINDING SITE FOR RESIDUE CA B 92
source : AC5

18) chain B
residue 23
type
sequence D
description BINDING SITE FOR RESIDUE CA B 92
source : AC5

19) chain B
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE CA B 92
source : AC5

20) chain B
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE CA B 92
source : AC5

21) chain B
residue 61
type
sequence D
description BINDING SITE FOR RESIDUE CA B 93
source : AC6

22) chain B
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE CA B 93
source : AC6

23) chain B
residue 65
type
sequence D
description BINDING SITE FOR RESIDUE CA B 93
source : AC6

24) chain B
residue 67
type
sequence E
description BINDING SITE FOR RESIDUE CA B 93
source : AC6

25) chain B
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CA B 93
source : AC6

26) chain B
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE S45 B 94
source : AC7

27) chain B
residue 45
type
sequence E
description BINDING SITE FOR RESIDUE S45 B 94
source : AC7

28) chain B
residue 56
type
sequence V
description BINDING SITE FOR RESIDUE S45 B 94
source : AC7

29) chain B
residue 76
type
sequence F
description BINDING SITE FOR RESIDUE S45 B 94
source : AC7

30) chain B
residue 79
type
sequence M
description BINDING SITE FOR RESIDUE S45 B 94
source : AC7

31) chain A
residue 63
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:2H61, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI4

32) chain B
residue 63
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:2H61, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI4

33) chain A
residue 1
type MOD_RES
sequence S
description N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638
source Swiss-Prot : SWS_FT_FI5

34) chain B
residue 1
type MOD_RES
sequence S
description N-acetylserine; alternate => ECO:0000250|UniProtKB:P02638
source Swiss-Prot : SWS_FT_FI5

35) chain A
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 65
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 67
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 72
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

39) chain B
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

40) chain B
residue 65
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

41) chain B
residue 67
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

42) chain B
residue 72
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 15
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

44) chain A
residue 25
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 85
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 15
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 25
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

48) chain B
residue 85
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

49) chain B
residue 90
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 18
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 31
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 21
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 23
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 26
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 31
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

56) chain B
residue 18
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

57) chain B
residue 21
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

58) chain B
residue 23
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

59) chain B
residue 26
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:20950652, ECO:0007744|PDB:3CZT, ECO:0007744|PDB:3D0Y, ECO:0007744|PDB:3D10
source Swiss-Prot : SWS_FT_FI2

60) chain A
residue 61-73
type prosite
sequence DNDGDGECDFQEF
description EF_HAND_1 EF-hand calcium-binding domain. DNDGDGECDfqEF
source prosite : PS00018

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


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