eF-site ID 3f19-A
PDB Code 3f19
Chain A

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Title Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor 4-fluoro-N-(2-nitroso-2-oxoethyl)benzenesulfonamide
Classification HYDROLASE
Compound Macrophage metalloelastase
Source Homo sapiens (Human) (MMP12_HUMAN)
Sequence A:  GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVT
PLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAF
GPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLG
LGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
Description


Functional site

1) chain A
residue 218
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 264
source : AC1

2) chain A
residue 222
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 264
source : AC1

3) chain A
residue 228
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 264
source : AC1

4) chain A
residue 168
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 265
source : AC2

5) chain A
residue 170
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 265
source : AC2

6) chain A
residue 183
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 265
source : AC2

7) chain A
residue 196
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 265
source : AC2

8) chain A
residue 158
type
sequence D
description BINDING SITE FOR RESIDUE CA A 266
source : AC3

9) chain A
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE CA A 266
source : AC3

10) chain A
residue 192
type
sequence G
description BINDING SITE FOR RESIDUE CA A 266
source : AC3

11) chain A
residue 194
type
sequence D
description BINDING SITE FOR RESIDUE CA A 266
source : AC3

12) chain A
residue 124
type
sequence D
description BINDING SITE FOR RESIDUE CA A 267
source : AC4

13) chain A
residue 199
type
sequence E
description BINDING SITE FOR RESIDUE CA A 267
source : AC4

14) chain A
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE CA A 267
source : AC4

15) chain A
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

16) chain A
residue 176
type
sequence G
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

17) chain A
residue 178
type
sequence G
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

18) chain A
residue 180
type
sequence I
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

19) chain A
residue 198
type
sequence D
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

20) chain A
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE CA A 268
source : AC5

21) chain A
residue 179
type
sequence G
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

22) chain A
residue 181
type
sequence L
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

23) chain A
residue 182
type
sequence A
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

24) chain A
residue 218
type
sequence H
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

25) chain A
residue 219
type
sequence E
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

26) chain A
residue 222
type
sequence H
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

27) chain A
residue 228
type
sequence H
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

28) chain A
residue 239
type
sequence T
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

29) chain A
residue 240
type
sequence Y
description BINDING SITE FOR RESIDUE HS6 A 0
source : AC6

30) chain A
residue 215-224
type prosite
sequence TAVHEIGHSL
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAVHEIGHSL
source prosite : PS00142

31) chain A
residue 219
type ACT_SITE
sequence E
description
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 124
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 190
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 192
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 194
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 196
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 198
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 199
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 201
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 218
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 222
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 228
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 158
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 168
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 170
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 175
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 176
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 178
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 180
type BINDING
sequence I
description
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 183
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2


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