eF-site ID 4b0t-AB
PDB Code 4b0t
Chain A, B

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Title Structure of the Pup Ligase PafA of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP
Classification LIGASE
Compound PUP--PROTEIN LIGASE
Source Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) (PAFA_CORGL)
Sequence A:  STVESALTRRIMGIETEYGLTFVDRPDEIARRMFRPIVEK
YSSSNIFIPNGSRLYLDVGSHPEYATAECDNLTQLINFEK
AGDVIADRMAVDAEESLAKEDIAGQVYLFKNNVDSVGNSY
GCHENYLVGRSMPLKALGKRLMPFLITRQLICGAGRIHHP
NPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINTR
DEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEM
IEADFGLPSLELANDIASIREISRDATGSTLLSLKDGTTM
TALQIQQVVFEHASKWLEQRPEPEFSGTSNTEMARVLDLW
GRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQRGNLGLD
DPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAIL
AAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNR
PEPQSVELGDPFSAVNSEVDQLIEYMTVHA
B:  STVESALTRRIMGIETEYGLTFVDLRPDEIARRMFRPIVE
KYSSSNIFIPNGSRLYLDVGSHPEYATAECDNLTQLINFE
KAGDVIADRMAVDAEESLAKEDIAGQVYLFKNNVDSVGNS
YGCHENYLVGRSMPLKALGKRLMPFLITRQLICGAGRIHH
PNPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINT
RDEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLE
MIEADFGLPSLELANDIASIREISRDATGSTLLSLKDGTT
MTALQIQQVVFEHASKWLEQRPEPEFSGTSNTEMARVLDL
WGRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQRGNLGL
DDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAI
LAAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVN
RPEPQSVELGDPFSAVNSEVDQLIEYMTVHAE
Description


Functional site

1) chain A
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

2) chain A
residue 73
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

3) chain A
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

4) chain A
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

5) chain A
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

6) chain A
residue 208
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

7) chain A
residue 210
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

8) chain A
residue 211
type
sequence H
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

9) chain A
residue 219
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

10) chain A
residue 418
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

11) chain A
residue 440
type
sequence W
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

12) chain A
residue 458
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

13) chain B
residue 12
type
sequence I
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

14) chain B
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

15) chain B
residue 15
type
sequence I
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

16) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

17) chain B
residue 444
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

18) chain B
residue 446
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

19) chain B
residue 450
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1478
source : AC1

20) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE MG A 1479
source : AC2

21) chain A
residue 14
type
sequence G
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

22) chain A
residue 15
type
sequence I
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

23) chain A
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

24) chain B
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

25) chain B
residue 73
type
sequence T
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

26) chain B
residue 74
type
sequence A
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

27) chain B
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

28) chain B
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

29) chain B
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

30) chain B
residue 210
type
sequence P
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

31) chain B
residue 211
type
sequence H
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

32) chain B
residue 219
type
sequence R
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

33) chain B
residue 418
type
sequence R
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

34) chain B
residue 440
type
sequence W
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

35) chain B
residue 458
type
sequence P
description BINDING SITE FOR RESIDUE ADP B 1479
source : AC3

36) chain A
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE MG B 1480
source : AC4

37) chain A
residue 64
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000305|PubMed:22910360
source Swiss-Prot : SWS_FT_FI1

38) chain B
residue 64
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000305|PubMed:22910360
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 16
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

40) chain B
residue 70
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 73
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 440
type BINDING
sequence W
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 60
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 62
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 70
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 73
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 440
type BINDING
sequence W
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 16
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 60
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 62
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_02111, ECO:0000269|PubMed:23601177
source Swiss-Prot : SWS_FT_FI2


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