eF-site ID 3cr3-A
PDB Code 3cr3
Chain A

click to enlarge
Title Structure of a transient complex between Dha-kinase subunits DhaM and DhaL from Lactococcus lactis
Classification TRANSFERASE
Compound PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL
Source Lactococcus lactis subsp. lactis (Streptococcus lactis) (DHAM_LACLA)
Sequence A:  LLTIDTTIEWLGKFNEKIQENKAYLSELDGPIGDGDHGAN
XARGXSETXKALEVSNFGNVSEIFKKVAXTLXSKVGGASG
PLYGSAFLAXSKTAIETLDTSELIYAGLEAIQKRGKAQVG
EKTXVDIWSAFLNDLQTDSASKDNLEKVVKASAGLLATKG
RASYLGERSIGHIDPGTQSSAYLFETLLEVVA
Description (1)  PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL, PTS-dependent dihydroxyacetone kinase, phosphotransferase subunit dhaM


Functional site

1) chain A
residue 29
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1212
source : AC3

2) chain A
residue 34
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1212
source : AC3

3) chain A
residue 36
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1212
source : AC3

4) chain A
residue 34
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1213
source : AC4

5) chain A
residue 36
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1213
source : AC4

6) chain A
residue 29
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

7) chain A
residue 34
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

8) chain A
residue 36
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

9) chain A
residue 37
type
sequence H
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

10) chain A
residue 40
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

11) chain A
residue 77
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

12) chain A
residue 78
type
sequence A
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

13) chain A
residue 79
type
sequence S
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

14) chain A
residue 82
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

15) chain A
residue 115
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

16) chain A
residue 117
type
sequence A
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

17) chain A
residue 123
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

18) chain A
residue 160
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

19) chain A
residue 161
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

20) chain A
residue 174
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

21) chain A
residue 175
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

22) chain A
residue 176
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1211
source : AC6

23) chain A
residue 161
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:18957416
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 36
type ACT_SITE
sequence D
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 37
type ACT_SITE
sequence H
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 78
type ACT_SITE
sequence A
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 115
type ACT_SITE
sequence G
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 124
type ACT_SITE
sequence X
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 174
type ACT_SITE
sequence D
description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419
source Swiss-Prot : SWS_FT_FI1


Display surface

Download
Links