eF-site ID 4ear-ABC
PDB Code 4ear
Chain A, B, C

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Title Crystal structure of purine nucleoside phosphorylase (W16Y, W94Y, W178Y, H257W) mutant from human complexed with DADMe-ImmG and phosphate
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound Purine nucleoside phosphorylase
Source Homo sapiens (Human) (PNPH_HUMAN)
Sequence A:  GYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDKLT
QAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQG
RFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLNPK
FEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMS
DAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFETV
AECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITN
KVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMASIP
LPD
B:  ENGYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDK
LTQAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMM
QGRFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLN
PKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPA
MSDAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFE
TVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLI
TNKVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMAS
IPLPDKA
C:  GYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDKLT
QAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQG
RFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLNPK
FEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMS
DAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFETV
AECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITN
KVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMASIP
LPDKA
Description (1)  Purine nucleoside phosphorylase (E.C.2.4.2.1)


Functional site

1) chain A
residue 33
type
sequence S
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

2) chain A
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

3) chain A
residue 88
type
sequence Y
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

4) chain A
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

5) chain A
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

6) chain A
residue 195
type
sequence V
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

7) chain A
residue 200
type
sequence F
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

8) chain A
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

9) chain A
residue 217
type
sequence V
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

10) chain A
residue 218
type
sequence G
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

11) chain A
residue 219
type
sequence M
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

12) chain A
residue 242
type
sequence T
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

13) chain A
residue 243
type
sequence N
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

14) chain A
residue 257
type
sequence X
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

15) chain C
residue 159
type
sequence F
description BINDING SITE FOR RESIDUE IM5 A 301
source : AC1

16) chain A
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

17) chain A
residue 33
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

18) chain A
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

19) chain A
residue 84
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

20) chain A
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

21) chain A
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

22) chain A
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

23) chain A
residue 220
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 302
source : AC2

24) chain B
residue 88
type
sequence Y
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

25) chain B
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

26) chain B
residue 117
type
sequence A
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

27) chain B
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

28) chain B
residue 195
type
sequence V
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

29) chain B
residue 200
type
sequence F
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

30) chain B
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

31) chain B
residue 217
type
sequence V
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

32) chain B
residue 218
type
sequence G
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

33) chain B
residue 219
type
sequence M
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

34) chain B
residue 242
type
sequence T
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

35) chain B
residue 243
type
sequence N
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

36) chain B
residue 257
type
sequence X
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

37) chain B
residue 260
type
sequence V
description BINDING SITE FOR RESIDUE IM5 B 301
source : AC3

38) chain B
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

39) chain B
residue 33
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

40) chain B
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

41) chain B
residue 84
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

42) chain B
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

43) chain B
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

44) chain B
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

45) chain B
residue 220
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 302
source : AC4

46) chain B
residue 159
type
sequence F
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

47) chain C
residue 33
type
sequence S
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

48) chain C
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

49) chain C
residue 88
type
sequence Y
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

50) chain C
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

51) chain C
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

52) chain C
residue 195
type
sequence V
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

53) chain C
residue 200
type
sequence F
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

54) chain C
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

55) chain C
residue 217
type
sequence V
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

56) chain C
residue 218
type
sequence G
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

57) chain C
residue 219
type
sequence M
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

58) chain C
residue 242
type
sequence T
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

59) chain C
residue 243
type
sequence N
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

60) chain C
residue 257
type
sequence X
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

61) chain C
residue 260
type
sequence V
description BINDING SITE FOR RESIDUE IM5 C 301
source : AC5

62) chain C
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

63) chain C
residue 33
type
sequence S
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

64) chain C
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

65) chain C
residue 84
type
sequence R
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

66) chain C
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

67) chain C
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

68) chain C
residue 116
type
sequence A
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

69) chain C
residue 220
type
sequence S
description BINDING SITE FOR RESIDUE PO4 C 302
source : AC6

70) chain A
residue 33
type catalytic
sequence S
description 17
source MCSA : MCSA1

71) chain A
residue 257
type catalytic
sequence X
description 17
source MCSA : MCSA1

72) chain A
residue 64
type catalytic
sequence H
description 17
source MCSA : MCSA1

73) chain A
residue 86
type catalytic
sequence H
description 17
source MCSA : MCSA1

74) chain A
residue 88
type catalytic
sequence Y
description 17
source MCSA : MCSA1

75) chain A
residue 89
type catalytic
sequence E
description 17
source MCSA : MCSA1

76) chain A
residue 116
type catalytic
sequence A
description 17
source MCSA : MCSA1

77) chain A
residue 219
type catalytic
sequence M
description 17
source MCSA : MCSA1

78) chain A
residue 220
type catalytic
sequence S
description 17
source MCSA : MCSA1

79) chain A
residue 243
type catalytic
sequence N
description 17
source MCSA : MCSA1

80) chain B
residue 33
type catalytic
sequence S
description 17
source MCSA : MCSA2

81) chain B
residue 257
type catalytic
sequence X
description 17
source MCSA : MCSA2

82) chain B
residue 64
type catalytic
sequence H
description 17
source MCSA : MCSA2

83) chain B
residue 86
type catalytic
sequence H
description 17
source MCSA : MCSA2

84) chain B
residue 88
type catalytic
sequence Y
description 17
source MCSA : MCSA2

85) chain B
residue 89
type catalytic
sequence E
description 17
source MCSA : MCSA2

86) chain B
residue 116
type catalytic
sequence A
description 17
source MCSA : MCSA2

87) chain B
residue 219
type catalytic
sequence M
description 17
source MCSA : MCSA2

88) chain B
residue 220
type catalytic
sequence S
description 17
source MCSA : MCSA2

89) chain B
residue 243
type catalytic
sequence N
description 17
source MCSA : MCSA2

90) chain C
residue 33
type catalytic
sequence S
description 17
source MCSA : MCSA3

91) chain C
residue 257
type catalytic
sequence X
description 17
source MCSA : MCSA3

92) chain C
residue 64
type catalytic
sequence H
description 17
source MCSA : MCSA3

93) chain C
residue 86
type catalytic
sequence H
description 17
source MCSA : MCSA3

94) chain C
residue 88
type catalytic
sequence Y
description 17
source MCSA : MCSA3

95) chain C
residue 89
type catalytic
sequence E
description 17
source MCSA : MCSA3

96) chain C
residue 116
type catalytic
sequence A
description 17
source MCSA : MCSA3

97) chain C
residue 219
type catalytic
sequence M
description 17
source MCSA : MCSA3

98) chain C
residue 220
type catalytic
sequence S
description 17
source MCSA : MCSA3

99) chain C
residue 243
type catalytic
sequence N
description 17
source MCSA : MCSA3

100) chain A
residue 79-120
type prosite
sequence VMMQGRFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAG
GL
description PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypLykvTfpVrVfhllGvdt.LVvtNAaGGL
source prosite : PS01240

101) chain A
residue 33
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI1

102) chain B
residue 33
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI1

103) chain C
residue 33
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI1

104) chain A
residue 64
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P55859
source Swiss-Prot : SWS_FT_FI2

105) chain B
residue 64
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P55859
source Swiss-Prot : SWS_FT_FI2

106) chain C
residue 64
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P55859
source Swiss-Prot : SWS_FT_FI2

107) chain A
residue 84
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI3

108) chain B
residue 84
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI3

109) chain C
residue 84
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI3

110) chain A
residue 88
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8
source Swiss-Prot : SWS_FT_FI4

111) chain B
residue 88
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8
source Swiss-Prot : SWS_FT_FI4

112) chain C
residue 88
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8
source Swiss-Prot : SWS_FT_FI4

113) chain A
residue 116
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

114) chain C
residue 201
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

115) chain C
residue 220
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

116) chain C
residue 243
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

117) chain A
residue 201
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

118) chain A
residue 220
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

119) chain A
residue 243
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

120) chain B
residue 116
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

121) chain B
residue 201
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

122) chain B
residue 220
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

123) chain B
residue 243
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

124) chain C
residue 116
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
source Swiss-Prot : SWS_FT_FI5

125) chain A
residue 219
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

126) chain A
residue 257
type BINDING
sequence X
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

127) chain B
residue 219
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

128) chain B
residue 257
type BINDING
sequence X
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

129) chain C
residue 219
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

130) chain C
residue 257
type BINDING
sequence X
description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
source Swiss-Prot : SWS_FT_FI6

131) chain A
residue 243
type SITE
sequence N
description Important for substrate specificity => ECO:0000269|PubMed:9305964
source Swiss-Prot : SWS_FT_FI7

132) chain B
residue 243
type SITE
sequence N
description Important for substrate specificity => ECO:0000269|PubMed:9305964
source Swiss-Prot : SWS_FT_FI7

133) chain C
residue 243
type SITE
sequence N
description Important for substrate specificity => ECO:0000269|PubMed:9305964
source Swiss-Prot : SWS_FT_FI7

134) chain A
residue 251
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9

135) chain B
residue 251
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9

136) chain C
residue 251
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9


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