eF-site ID 1lna-E
PDB Code 1lna
Chain E

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Title A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN
Classification METALLOPROTEASE
Compound THERMOLYSIN
Source (THER_BACTH)
Sequence E:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIF
TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT
YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSEM
VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE
SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA
AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSN
FSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK
Description


Functional site

1) chain E
residue 166
type
sequence E
description
source : CO0

2) chain E
residue 142
type
sequence H
description
source : CO0

3) chain E
residue 146
type
sequence H
description
source : CO0

4) chain E
residue 112
type
sequence N
description BINDING SITE FOR RESIDUE VAL E 1321
source : AC1

5) chain E
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE VAL E 1321
source : AC1

6) chain E
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE VAL E 1321
source : AC1

7) chain E
residue 203
type
sequence R
description BINDING SITE FOR RESIDUE VAL E 1321
source : AC1

8) chain E
residue 111
type
sequence N
description BINDING SITE FOR RESIDUE LYS E 1322
source : AC2

9) chain E
residue 112
type
sequence N
description BINDING SITE FOR RESIDUE LYS E 1322
source : AC2

10) chain E
residue 231
type
sequence H
description BINDING SITE FOR RESIDUE LYS E 1322
source : AC2

11) chain E
residue 142
type
sequence H
description BINDING SITE FOR RESIDUE CO E 900
source : AC3

12) chain E
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE CO E 900
source : AC3

13) chain E
residue 166
type
sequence E
description BINDING SITE FOR RESIDUE CO E 900
source : AC3

14) chain E
residue 138
type
sequence D
description BINDING SITE FOR RESIDUE CA E 901
source : AC4

15) chain E
residue 177
type
sequence E
description BINDING SITE FOR RESIDUE CA E 901
source : AC4

16) chain E
residue 185
type
sequence D
description BINDING SITE FOR RESIDUE CA E 901
source : AC4

17) chain E
residue 187
type
sequence E
description BINDING SITE FOR RESIDUE CA E 901
source : AC4

18) chain E
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE CA E 901
source : AC4

19) chain E
residue 177
type
sequence E
description BINDING SITE FOR RESIDUE CA E 902
source : AC5

20) chain E
residue 183
type
sequence N
description BINDING SITE FOR RESIDUE CA E 902
source : AC5

21) chain E
residue 185
type
sequence D
description BINDING SITE FOR RESIDUE CA E 902
source : AC5

22) chain E
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE CA E 902
source : AC5

23) chain E
residue 57
type
sequence D
description BINDING SITE FOR RESIDUE CO E 903
source : AC6

24) chain E
residue 59
type
sequence D
description BINDING SITE FOR RESIDUE CO E 903
source : AC6

25) chain E
residue 61
type
sequence Q
description BINDING SITE FOR RESIDUE CO E 903
source : AC6

26) chain E
residue 193
type
sequence Y
description BINDING SITE FOR RESIDUE CA E 904
source : AC7

27) chain E
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE CA E 904
source : AC7

28) chain E
residue 197
type
sequence I
description BINDING SITE FOR RESIDUE CA E 904
source : AC7

29) chain E
residue 200
type
sequence D
description BINDING SITE FOR RESIDUE CA E 904
source : AC7

30) chain E
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE DMS E 320
source : AC8

31) chain E
residue 218
type
sequence S
description BINDING SITE FOR RESIDUE DMS E 320
source : AC8

32) chain E
residue 251
type
sequence Y
description BINDING SITE FOR RESIDUE DMS E 320
source : AC8

33) chain E
residue 139-148
type prosite
sequence VVAHELTHAV
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
source prosite : PS00142

34) chain E
residue 291
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI1

35) chain E
residue 289
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI1

36) chain E
residue 293
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI1


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