eF-site ID 1m9y-ABCDEFGH
PDB Code 1m9y
Chain A, B, C, D, E, F, G, H

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Title X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,G89A Complex.
Classification Isomerase/Viral protein
Compound Cyclophilin A
Source Homo sapiens (Human) (Q72497_9HIV1)
Sequence A:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS
TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
B:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST
GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE
KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW
LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC
GQLE
C:  PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMF
SALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW
DRLHPVAAAPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH
NPPIPVGEIYKRWIILGLNKIVRMYS
D:  HQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQD
LNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVAAAPI
APGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYK
RWIILGLNKIVRMYS
E:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS
TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
F:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST
GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE
KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW
LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC
GQLE
G:  PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMF
SALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW
DRLHPVAAAPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH
NPPIPVGEIYKRWIILGLNKIVRMYS
H:  HQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQD
LNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVAAAPI
APGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYK
RWIILGLNKIVRMYS
Description


Functional site

1) chain A
residue 55
type catalytic
sequence R
description 189
source MCSA : MCSA1

2) chain A
residue 60
type catalytic
sequence F
description 189
source MCSA : MCSA1

3) chain A
residue 63
type catalytic
sequence Q
description 189
source MCSA : MCSA1

4) chain A
residue 102
type catalytic
sequence N
description 189
source MCSA : MCSA1

5) chain A
residue 113
type catalytic
sequence F
description 189
source MCSA : MCSA1

6) chain A
residue 122
type catalytic
sequence L
description 189
source MCSA : MCSA1

7) chain A
residue 126
type catalytic
sequence H
description 189
source MCSA : MCSA1

8) chain B
residue 55
type catalytic
sequence R
description 189
source MCSA : MCSA2

9) chain B
residue 60
type catalytic
sequence F
description 189
source MCSA : MCSA2

10) chain B
residue 63
type catalytic
sequence Q
description 189
source MCSA : MCSA2

11) chain B
residue 102
type catalytic
sequence N
description 189
source MCSA : MCSA2

12) chain B
residue 113
type catalytic
sequence F
description 189
source MCSA : MCSA2

13) chain B
residue 122
type catalytic
sequence L
description 189
source MCSA : MCSA2

14) chain B
residue 126
type catalytic
sequence H
description 189
source MCSA : MCSA2

15) chain E
residue 55
type catalytic
sequence R
description 189
source MCSA : MCSA3

16) chain E
residue 60
type catalytic
sequence F
description 189
source MCSA : MCSA3

17) chain E
residue 63
type catalytic
sequence Q
description 189
source MCSA : MCSA3

18) chain E
residue 102
type catalytic
sequence N
description 189
source MCSA : MCSA3

19) chain E
residue 113
type catalytic
sequence F
description 189
source MCSA : MCSA3

20) chain E
residue 122
type catalytic
sequence L
description 189
source MCSA : MCSA3

21) chain E
residue 126
type catalytic
sequence H
description 189
source MCSA : MCSA3

22) chain F
residue 55
type catalytic
sequence R
description 189
source MCSA : MCSA4

23) chain F
residue 60
type catalytic
sequence F
description 189
source MCSA : MCSA4

24) chain F
residue 63
type catalytic
sequence Q
description 189
source MCSA : MCSA4

25) chain F
residue 102
type catalytic
sequence N
description 189
source MCSA : MCSA4

26) chain F
residue 113
type catalytic
sequence F
description 189
source MCSA : MCSA4

27) chain F
residue 122
type catalytic
sequence L
description 189
source MCSA : MCSA4

28) chain F
residue 126
type catalytic
sequence H
description 189
source MCSA : MCSA4

29) chain A
residue 48-65
type prosite
sequence YKGSCFHRIIPGFMCQGG
description CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
source prosite : PS00170

30) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI1

31) chain E
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 28
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
source Swiss-Prot : SWS_FT_FI10

33) chain B
residue 28
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
source Swiss-Prot : SWS_FT_FI10

34) chain E
residue 28
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
source Swiss-Prot : SWS_FT_FI10

35) chain F
residue 28
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
source Swiss-Prot : SWS_FT_FI10

36) chain A
residue 82
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

37) chain B
residue 82
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

38) chain E
residue 82
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

39) chain F
residue 82
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

40) chain A
residue 2
type MOD_RES
sequence V
description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 2
type MOD_RES
sequence V
description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2

42) chain E
residue 2
type MOD_RES
sequence V
description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2

43) chain F
residue 2
type MOD_RES
sequence V
description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 28
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

45) chain A
residue 82
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

46) chain B
residue 28
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

47) chain B
residue 82
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

48) chain E
residue 28
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

49) chain E
residue 82
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

50) chain F
residue 28
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

51) chain F
residue 82
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

52) chain A
residue 44
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

53) chain F
residue 44
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

54) chain F
residue 76
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

55) chain F
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

56) chain A
residue 76
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

57) chain A
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

58) chain B
residue 44
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

59) chain B
residue 76
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

60) chain B
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

61) chain E
residue 44
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

62) chain E
residue 76
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

63) chain E
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

64) chain A
residue 77
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

65) chain B
residue 77
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

66) chain E
residue 77
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

67) chain F
residue 77
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

68) chain A
residue 93
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6

69) chain B
residue 93
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6

70) chain E
residue 93
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6

71) chain F
residue 93
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6

72) chain A
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

73) chain B
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

74) chain E
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

75) chain F
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

76) chain A
residue 133
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17742
source Swiss-Prot : SWS_FT_FI8

77) chain B
residue 133
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17742
source Swiss-Prot : SWS_FT_FI8

78) chain E
residue 133
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17742
source Swiss-Prot : SWS_FT_FI8

79) chain F
residue 133
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17742
source Swiss-Prot : SWS_FT_FI8

80) chain A
residue 108
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

81) chain B
residue 108
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

82) chain E
residue 108
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

83) chain F
residue 108
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI9


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