eF-site ID 5f34-ABCD
PDB Code 5f34
Chain A, B, C, D

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Title Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with S-hexadecyl Coenzyme A - P21 space group
Classification TRANSFERASE
Compound Phosphatidylinositol mannoside acyltransferase
Source Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (ACYLT_MYCS2)
Sequence A:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR
LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN
WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF
EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ
VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR
VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ
WIADLSDERRARL
B:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR
LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN
WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF
EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ
VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR
VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ
WIADLSDERRARL
C:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR
LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN
WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF
EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ
VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR
VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ
WIADLSDERRAR
D:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR
LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN
WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF
EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ
VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR
VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ
WIADLSDERRARL
Description


Functional site

1) chain A
residue 122
type
sequence L
description binding site for residue HD6 A 401
source : AC1

2) chain A
residue 124
type
sequence L
description binding site for residue HD6 A 401
source : AC1

3) chain A
residue 130
type
sequence W
description binding site for residue HD6 A 401
source : AC1

4) chain A
residue 146
type
sequence T
description binding site for residue HD6 A 401
source : AC1

5) chain A
residue 147
type
sequence V
description binding site for residue HD6 A 401
source : AC1

6) chain A
residue 164
type
sequence R
description binding site for residue HD6 A 401
source : AC1

7) chain A
residue 182
type
sequence F
description binding site for residue HD6 A 401
source : AC1

8) chain A
residue 196
type
sequence C
description binding site for residue HD6 A 401
source : AC1

9) chain A
residue 198
type
sequence M
description binding site for residue HD6 A 401
source : AC1

10) chain A
residue 206
type
sequence S
description binding site for residue HD6 A 401
source : AC1

11) chain A
residue 220
type
sequence P
description binding site for residue HD6 A 401
source : AC1

12) chain A
residue 222
type
sequence G
description binding site for residue HD6 A 401
source : AC1

13) chain A
residue 229
type
sequence E
description binding site for residue HD6 A 401
source : AC1

14) chain B
residue 130
type
sequence W
description binding site for residue HD6 B 401
source : AC2

15) chain B
residue 133
type
sequence A
description binding site for residue HD6 B 401
source : AC2

16) chain B
residue 134
type
sequence G
description binding site for residue HD6 B 401
source : AC2

17) chain B
residue 146
type
sequence T
description binding site for residue HD6 B 401
source : AC2

18) chain B
residue 147
type
sequence V
description binding site for residue HD6 B 401
source : AC2

19) chain B
residue 149
type
sequence E
description binding site for residue HD6 B 401
source : AC2

20) chain B
residue 164
type
sequence R
description binding site for residue HD6 B 401
source : AC2

21) chain B
residue 196
type
sequence C
description binding site for residue HD6 B 401
source : AC2

22) chain B
residue 198
type
sequence M
description binding site for residue HD6 B 401
source : AC2

23) chain B
residue 220
type
sequence P
description binding site for residue HD6 B 401
source : AC2

24) chain B
residue 222
type
sequence G
description binding site for residue HD6 B 401
source : AC2

25) chain C
residue 124
type
sequence L
description binding site for residue HD6 C 401
source : AC3

26) chain C
residue 130
type
sequence W
description binding site for residue HD6 C 401
source : AC3

27) chain C
residue 133
type
sequence A
description binding site for residue HD6 C 401
source : AC3

28) chain C
residue 134
type
sequence G
description binding site for residue HD6 C 401
source : AC3

29) chain C
residue 196
type
sequence C
description binding site for residue HD6 C 401
source : AC3

30) chain C
residue 198
type
sequence M
description binding site for residue HD6 C 401
source : AC3

31) chain C
residue 202
type
sequence D
description binding site for residue HD6 C 401
source : AC3

32) chain C
residue 220
type
sequence P
description binding site for residue HD6 C 401
source : AC3

33) chain C
residue 222
type
sequence G
description binding site for residue HD6 C 401
source : AC3

34) chain D
residue 130
type
sequence W
description binding site for residue HD6 D 401
source : AC4

35) chain D
residue 146
type
sequence T
description binding site for residue HD6 D 401
source : AC4

36) chain D
residue 147
type
sequence V
description binding site for residue HD6 D 401
source : AC4

37) chain D
residue 149
type
sequence E
description binding site for residue HD6 D 401
source : AC4

38) chain D
residue 164
type
sequence R
description binding site for residue HD6 D 401
source : AC4

39) chain D
residue 182
type
sequence F
description binding site for residue HD6 D 401
source : AC4

40) chain D
residue 196
type
sequence C
description binding site for residue HD6 D 401
source : AC4

41) chain D
residue 198
type
sequence M
description binding site for residue HD6 D 401
source : AC4

42) chain D
residue 201
type
sequence R
description binding site for residue HD6 D 401
source : AC4

43) chain D
residue 202
type
sequence D
description binding site for residue HD6 D 401
source : AC4

44) chain D
residue 220
type
sequence P
description binding site for residue HD6 D 401
source : AC4

45) chain D
residue 222
type
sequence G
description binding site for residue HD6 D 401
source : AC4

46) chain A
residue 126
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 126
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI1

48) chain C
residue 126
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI1

49) chain D
residue 126
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 200
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 200
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI2

52) chain C
residue 200
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI2

53) chain D
residue 200
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 126
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

55) chain C
residue 164
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

56) chain C
residue 206
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

57) chain C
residue 229
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

58) chain D
residue 126
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

59) chain D
residue 164
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

60) chain D
residue 206
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

61) chain D
residue 229
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

62) chain A
residue 164
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

63) chain A
residue 206
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

64) chain A
residue 229
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

65) chain B
residue 126
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

66) chain B
residue 164
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

67) chain B
residue 206
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

68) chain B
residue 229
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3

69) chain C
residue 126
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26965057
source Swiss-Prot : SWS_FT_FI3


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