eF-site ID 1d09-ABCD
PDB Code 1d09
Chain A, B, C, D

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Title ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)
Classification TRANSFERASE
Compound ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN
Source Escherichia coli (strain K12) (PYRI_ECOLI)
Sequence A:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK
HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG
NVPVLNAGDGSNQHPTQTLLDLFTIQQTQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT
PHAWYFQQAGNGIFARQALLALVLNRDLVL
B:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ
RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ
ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP
VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN
C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK
HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG
NVPVLNAGDGSNQHPTQTLLDLFTIQQTQGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT
PHAWYFQQAGNGIFARQALLALVLNRDLVL
D:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ
RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ
ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP
VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN
Description


Functional site

1) chain B
residue 109
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1313
source : AC1

2) chain B
residue 114
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1313
source : AC1

3) chain B
residue 138
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1313
source : AC1

4) chain B
residue 141
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1313
source : AC1

5) chain D
residue 109
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 1314
source : AC2

6) chain D
residue 114
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 1314
source : AC2

7) chain D
residue 138
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 1314
source : AC2

8) chain D
residue 141
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 1314
source : AC2

9) chain A
residue 52
type
sequence S
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

10) chain A
residue 53
type
sequence T
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

11) chain A
residue 54
type
sequence R
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

12) chain A
residue 55
type
sequence T
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

13) chain A
residue 80
type
sequence S
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

14) chain A
residue 84
type
sequence K
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

15) chain A
residue 105
type
sequence R
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

16) chain A
residue 134
type
sequence H
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

17) chain A
residue 137
type
sequence Q
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

18) chain A
residue 167
type
sequence R
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

19) chain A
residue 229
type
sequence R
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

20) chain A
residue 231
type
sequence Q
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

21) chain A
residue 267
type
sequence L
description BINDING SITE FOR RESIDUE PAL A 1311
source : AC3

22) chain C
residue 52
type
sequence S
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

23) chain C
residue 53
type
sequence T
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

24) chain C
residue 54
type
sequence R
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

25) chain C
residue 55
type
sequence T
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

26) chain C
residue 80
type
sequence S
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

27) chain C
residue 84
type
sequence K
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

28) chain C
residue 105
type
sequence R
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

29) chain C
residue 134
type
sequence H
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

30) chain C
residue 167
type
sequence R
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

31) chain C
residue 168
type
sequence T
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

32) chain C
residue 229
type
sequence R
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

33) chain C
residue 267
type
sequence L
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

34) chain C
residue 268
type
sequence P
description BINDING SITE FOR RESIDUE PAL C 1312
source : AC4

35) chain A
residue 54
type catalytic
sequence R
description 405
source MCSA : MCSA1

36) chain A
residue 55
type catalytic
sequence T
description 405
source MCSA : MCSA1

37) chain A
residue 84
type catalytic
sequence K
description 405
source MCSA : MCSA1

38) chain A
residue 105
type catalytic
sequence R
description 405
source MCSA : MCSA1

39) chain A
residue 134
type catalytic
sequence H
description 405
source MCSA : MCSA1

40) chain C
residue 54
type catalytic
sequence R
description 405
source MCSA : MCSA2

41) chain C
residue 55
type catalytic
sequence T
description 405
source MCSA : MCSA2

42) chain C
residue 84
type catalytic
sequence K
description 405
source MCSA : MCSA2

43) chain C
residue 105
type catalytic
sequence R
description 405
source MCSA : MCSA2

44) chain C
residue 134
type catalytic
sequence H
description 405
source MCSA : MCSA2

45) chain A
residue 48-55
type prosite
sequence FFEASTRT
description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT
source prosite : PS00097

46) chain B
residue 109
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

47) chain C
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

48) chain C
residue 134
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

49) chain C
residue 137
type BINDING
sequence Q
description
source Swiss-Prot : SWS_FT_FI1

50) chain C
residue 267
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI1

51) chain C
residue 268
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI1

52) chain B
residue 114
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 138
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 141
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

55) chain D
residue 109
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

56) chain D
residue 114
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

57) chain D
residue 138
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

58) chain D
residue 141
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

59) chain C
residue 55
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 84
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 167
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

62) chain A
residue 229
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

63) chain C
residue 84
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

64) chain C
residue 167
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

65) chain C
residue 229
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2


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