eF-site ID 5dir-A
PDB Code 5dir
Chain A

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Title membrane protein at 2.8 Angstroms
Classification HYDROLASE
Compound Lipoprotein signal peptidase
Source (5DIR)
Sequence A:  PDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIV
VIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVS
ASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGH
VVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMF
Description


Functional site

1) chain A
residue 100
type
sequence I
description binding site for residue OLC A 201
source : AC1

2) chain A
residue 139
type
sequence F
description binding site for residue OLC A 201
source : AC1

3) chain A
residue 143
type
sequence D
description binding site for residue OLC A 201
source : AC1

4) chain A
residue 147
type
sequence T
description binding site for residue OLC A 201
source : AC1

5) chain A
residue 148
type
sequence V
description binding site for residue OLC A 201
source : AC1

6) chain A
residue 26
type
sequence S
description binding site for residue OLC A 202
source : AC2

7) chain A
residue 29
type
sequence F
description binding site for residue OLC A 202
source : AC2

8) chain A
residue 33
type
sequence E
description binding site for residue OLC A 202
source : AC2

9) chain A
residue 40
type
sequence I
description binding site for residue OLC A 202
source : AC2

10) chain A
residue 49
type
sequence W
description binding site for residue OLC A 202
source : AC2

11) chain A
residue 141
type
sequence L
description binding site for residue OLC A 202
source : AC2

12) chain A
residue 41
type
sequence V
description binding site for residue OLC A 203
source : AC3

13) chain A
residue 49
type
sequence W
description binding site for residue OLC A 203
source : AC3

14) chain A
residue 4
type
sequence V
description binding site for residue OLC A 204
source : AC4

15) chain A
residue 8
type
sequence G
description binding site for residue OLC A 204
source : AC4

16) chain A
residue 11
type
sequence P
description binding site for residue OLC A 204
source : AC4

17) chain A
residue 12
type
sequence W
description binding site for residue OLC A 204
source : AC4

18) chain A
residue 15
type
sequence I
description binding site for residue OLC A 204
source : AC4

19) chain A
residue 93
type
sequence K
description binding site for residue OLC A 204
source : AC4

20) chain A
residue 10
type
sequence L
description binding site for residue OLC A 205
source : AC5

21) chain A
residue 11
type
sequence P
description binding site for residue OLC A 205
source : AC5

22) chain A
residue 14
type
sequence W
description binding site for residue OLC A 205
source : AC5

23) chain A
residue 20
type
sequence F
description binding site for residue OLC A 205
source : AC5

24) chain A
residue 20
type
sequence F
description binding site for residue OLC A 206
source : AC6

25) chain A
residue 70
type
sequence R
description binding site for residue OLC A 206
source : AC6

26) chain A
residue 117
type
sequence M
description binding site for residue OLC A 206
source : AC6

27) chain A
residue 63
type
sequence A
description binding site for residue OLC B 206
source : AD3

28) chain A
residue 64
type
sequence D
description binding site for residue OLC B 206
source : AD3

29) chain A
residue 65
type
sequence S
description binding site for residue OLC B 206
source : AD3

30) chain A
residue 71
type
sequence W
description binding site for residue OLC B 206
source : AD3

31) chain A
residue 54
type
sequence N
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

32) chain A
residue 59
type
sequence F
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

33) chain A
residue 62
type
sequence L
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

34) chain A
residue 72
type
sequence L
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

35) chain A
residue 73
type
sequence F
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

36) chain A
residue 112
type
sequence N
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

37) chain A
residue 116
type
sequence R
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

38) chain A
residue 122
type
sequence V
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

39) chain A
residue 124
type
sequence D
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

40) chain A
residue 140
type
sequence N
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

41) chain A
residue 143
type
sequence D
description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
source : AE7

42) chain A
residue 105-117
type prosite
sequence VLGGALGNLYDRM
description SPASE_II Signal peptidases II signature. VlGGALGNLYDRM
source prosite : PS00855

43) chain A
residue 31-67
type TOPO_DOM
sequence QAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG
description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 119-140
type TOPO_DOM
sequence LGHVVDFILVHWQNRWYFPAFN
description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI3

45) chain A
residue 68-89
type TRANSMEM
sequence WQRWLFALIAIVVSASLVVWLK
description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI4

46) chain A
residue 97-118
type TRANSMEM
sequence WLAIALALVLGGALGNLYDRMV
description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 141-154
type TRANSMEM
sequence LADSAITVGAVMLA
description Helical => ECO:0000269|PubMed:26912896, ECO:0007744|PDB:5DIR
source Swiss-Prot : SWS_FT_FI5

48) chain A
residue 124
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896
source Swiss-Prot : SWS_FT_FI7

49) chain A
residue 143
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896
source Swiss-Prot : SWS_FT_FI7

50) chain A
residue 90-96
type TOPO_DOM
sequence RLKKGET
description Cytoplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI1

51) chain A
residue 10-30
type TRANSMEM
sequence LPWLWITVLVFVLDQVSKAFF
description Helical => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
source Swiss-Prot : SWS_FT_FI2


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