eF-site ID 3jzi-AB
PDB Code 3jzi
Chain A, B

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Title Crystal structure of biotin carboxylase from E. Coli in complex with benzimidazole series
Classification LIGASE
Compound Biotin carboxylase
Source Escherichia coli (strain K12) (ACCC_ECOLI)
Sequence A:  MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLK
HVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP
GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI
AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKA
SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYM
EKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV
EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE
NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP
LSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP
GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIA
RMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYL
EKKLG
B:  RHMLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRD
LKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAI
HPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVS
AIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVII
KASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMV
YMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQK
VVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFL
FENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAG
QPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFH
APGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA
IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIH
YLEKKL
Description


Functional site

1) chain A
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

2) chain A
residue 159
type
sequence K
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

3) chain A
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

4) chain A
residue 164
type
sequence G
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

5) chain A
residue 165
type
sequence G
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

6) chain A
residue 167
type
sequence R
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

7) chain A
residue 169
type
sequence M
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

8) chain A
residue 199
type
sequence Y
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

9) chain A
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

10) chain A
residue 202
type
sequence K
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

11) chain A
residue 203
type
sequence Y
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

12) chain A
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

13) chain A
residue 209
type
sequence H
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

14) chain A
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

15) chain A
residue 236
type
sequence H
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

16) chain A
residue 278
type
sequence L
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

17) chain A
residue 287
type
sequence I
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

18) chain A
residue 288
type
sequence E
description BINDING SITE FOR RESIDUE JZL A 466
source : AC1

19) chain B
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

20) chain B
residue 157
type
sequence I
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

21) chain B
residue 159
type
sequence K
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

22) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

23) chain B
residue 164
type
sequence G
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

24) chain B
residue 165
type
sequence G
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

25) chain B
residue 167
type
sequence R
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

26) chain B
residue 168
type
sequence G
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

27) chain B
residue 169
type
sequence M
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

28) chain B
residue 199
type
sequence Y
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

29) chain B
residue 201
type
sequence E
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

30) chain B
residue 202
type
sequence K
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

31) chain B
residue 203
type
sequence Y
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

32) chain B
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

33) chain B
residue 209
type
sequence H
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

34) chain B
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

35) chain B
residue 236
type
sequence H
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

36) chain B
residue 278
type
sequence L
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

37) chain B
residue 287
type
sequence I
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

38) chain B
residue 288
type
sequence E
description BINDING SITE FOR RESIDUE JZL B 466
source : AC2

39) chain A
residue 154-168
type prosite
sequence YPVIIKASGGGGGRG
description CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG
source prosite : PS00866

40) chain A
residue 286-293
type prosite
sequence FIEMNTRI
description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI
source prosite : PS00867

41) chain A
residue 292
type ACT_SITE
sequence R
description ACT_SITE => ECO:0000269|PubMed:19213731
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 292
type ACT_SITE
sequence R
description ACT_SITE => ECO:0000269|PubMed:19213731
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 116
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 165
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 116
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 165
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 159
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI3

48) chain B
residue 159
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 201
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI4

50) chain B
residue 201
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D
source Swiss-Prot : SWS_FT_FI4

51) chain A
residue 209
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

52) chain B
residue 338
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

53) chain A
residue 238
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

54) chain A
residue 292
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

55) chain A
residue 295
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

56) chain A
residue 338
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

57) chain B
residue 209
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

58) chain B
residue 238
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

59) chain B
residue 292
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

60) chain B
residue 295
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI5

61) chain A
residue 236
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI6

62) chain B
residue 236
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C
source Swiss-Prot : SWS_FT_FI6

63) chain A
residue 276
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7

64) chain A
residue 288
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7

65) chain A
residue 290
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7

66) chain B
residue 276
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7

67) chain B
residue 288
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7

68) chain B
residue 290
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409
source Swiss-Prot : SWS_FT_FI7


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