eF-site ID 6qk6_15-A
PDB Code 6qk6
Model 15
Chain A

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Title Solution Structure of the Cd-loaded form of a Metallothionein from Helix Pomatia
Classification METAL BINDING PROTEIN
Compound Cadmium-metallothionein
Source (MTCD_HELPO)
Sequence A:  GSGKGKGEKCTSACRSEPCQCGSKCQCGEGCTCAACKTCN
CTSDGCKCGKECTGPDSCKCGSSCSCK
Description


Functional site

1) chain A
residue 10
type
sequence C
description binding site for residue CD A 101
source : AC1

2) chain A
residue 14
type
sequence C
description binding site for residue CD A 101
source : AC1

3) chain A
residue 27
type
sequence C
description binding site for residue CD A 101
source : AC1

4) chain A
residue 31
type
sequence C
description binding site for residue CD A 101
source : AC1

5) chain A
residue 14
type
sequence C
description binding site for residue CD A 102
source : AC2

6) chain A
residue 19
type
sequence C
description binding site for residue CD A 102
source : AC2

7) chain A
residue 33
type
sequence C
description binding site for residue CD A 102
source : AC2

8) chain A
residue 36
type
sequence C
description binding site for residue CD A 102
source : AC2

9) chain A
residue 21
type
sequence C
description binding site for residue CD A 103
source : AC3

10) chain A
residue 25
type
sequence C
description binding site for residue CD A 103
source : AC3

11) chain A
residue 27
type
sequence C
description binding site for residue CD A 103
source : AC3

12) chain A
residue 36
type
sequence C
description binding site for residue CD A 103
source : AC3

13) chain A
residue 39
type
sequence C
description binding site for residue CD A 104
source : AC4

14) chain A
residue 52
type
sequence C
description binding site for residue CD A 104
source : AC4

15) chain A
residue 58
type
sequence C
description binding site for residue CD A 104
source : AC4

16) chain A
residue 66
type
sequence C
description binding site for residue CD A 104
source : AC4

17) chain A
residue 67
type
sequence K
description binding site for residue CD A 104
source : AC4

18) chain A
residue 48
type
sequence C
description binding site for residue CD A 105
source : AC5

19) chain A
residue 50
type
sequence K
description binding site for residue CD A 105
source : AC5

20) chain A
residue 60
type
sequence C
description binding site for residue CD A 105
source : AC5

21) chain A
residue 64
type
sequence C
description binding site for residue CD A 105
source : AC5

22) chain A
residue 66
type
sequence C
description binding site for residue CD A 105
source : AC5

23) chain A
residue 41
type
sequence C
description binding site for residue CD A 106
source : AC6

24) chain A
residue 46
type
sequence C
description binding site for residue CD A 106
source : AC6

25) chain A
residue 48
type
sequence C
description binding site for residue CD A 106
source : AC6

26) chain A
residue 49
type
sequence G
description binding site for residue CD A 106
source : AC6

27) chain A
residue 52
type
sequence C
description binding site for residue CD A 106
source : AC6

28) chain A
residue 2
type MOD_RES
sequence S
description N-acetylserine => ECO:0000269|PubMed:8404892
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 39
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 41
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 46
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 48
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 52
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

34) chain A
residue 58
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 60
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

36) chain A
residue 64
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 66
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 19
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 21
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 25
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 27
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 31
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 33
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

44) chain A
residue 36
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 14
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1

46) chain A
residue 10
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:31633358, ECO:0007744|PDB:6QK6
source Swiss-Prot : SWS_FT_FI1


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