eF-site ID 2hry-A
PDB Code 2hry
Chain A

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Title T. maritima PurL complexed with AMPPCP
Classification LIGASE
Compound Phosphoribosylformylglycinamidine synthase II
Source Thermotoga maritima (PURL_THEMA)
Sequence A:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY
IRRLPKTGVVNLDDYYSVAFKIESANHPSAIEPYNGAATG
VGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEGIADYGN
SIGVPTVGGELRISSLYAHNPLVNVLAAGVVRNDMLVDSK
ASRPGQVIVIFGGATGRDGIVGDPFAEKMLIEAFLEMVEE
GLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLDRVPLRE
PDMEPWEILISESQERMAVVTSPQKASRILEIARKHLLFG
DVVAEVIEEPVYRVMYRNDLVMEVPVQLLANAPEEDIVEY
TPGKIPEFKRVEFEEVNAREVFEQYDHMVGTDTVVPPGFG
AAVMRIKRDGGYSLVTHSRADLALQDTYWGTLIAVLESVR
KTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTALKNACE
FSGVPVASGNASLYNTYQGKPIPPTLVVGMLGKVNPQKVA
KPKPSKVFAVGWNDFELEREKELWRAIRKLSEEGAFILSS
SQLLTRTHVETFREYGLKIEVKLPEVRPAHQMVLVFSERT
PVVDVPVKEIGTLSR
Description


Functional site

1) chain A
residue 32
type
sequence H
description BINDING SITE FOR RESIDUE MG A 901
source : AC1

2) chain A
residue 33
type
sequence C
description BINDING SITE FOR RESIDUE MG A 901
source : AC1

3) chain A
residue 94
type
sequence D
description BINDING SITE FOR RESIDUE MG A 902
source : AC2

4) chain A
residue 236
type
sequence D
description BINDING SITE FOR RESIDUE MG A 902
source : AC2

5) chain A
residue 139
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

6) chain A
residue 405
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

7) chain A
residue 429
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

8) chain A
residue 547
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

9) chain A
residue 548
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

10) chain A
residue 549
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 905
source : AC3

11) chain A
residue 32
type
sequence H
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

12) chain A
residue 35
type
sequence Y
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

13) chain A
residue 42
type
sequence I
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

14) chain A
residue 68
type
sequence K
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

15) chain A
residue 70
type
sequence E
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

16) chain A
residue 94
type
sequence D
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

17) chain A
residue 238
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

18) chain A
residue 239
type
sequence A
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

19) chain A
residue 442
type
sequence N
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

20) chain A
residue 474
type
sequence V
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

21) chain A
residue 476
type
sequence S
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

22) chain A
residue 477
type
sequence G
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

23) chain A
residue 478
type
sequence N
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

24) chain A
residue 479
type
sequence A
description BINDING SITE FOR RESIDUE ACP A 900
source : AC4

25) chain A
residue 72
type ACT_SITE
sequence A
description Proton acceptor => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 32
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 107
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI6

28) chain A
residue 388
type BINDING
sequence G
description BINDING => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI6

29) chain A
residue 429
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI6

30) chain A
residue 549
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI6

31) chain A
residue 556
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:17154526
source Swiss-Prot : SWS_FT_FI6

32) chain A
residue 477
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
source Swiss-Prot : SWS_FT_FI7

33) chain A
residue 35
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 68
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 442
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 70
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 94
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
source Swiss-Prot : SWS_FT_FI4

38) chain A
residue 236
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
source Swiss-Prot : SWS_FT_FI4

39) chain A
residue 478
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526
source Swiss-Prot : SWS_FT_FI4

40) chain A
residue 246-258
type prosite
sequence TSELVAKGNLGAI
description PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI
source prosite : PS01023

41) chain A
residue 71
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI5

42) chain A
residue 93
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI5

43) chain A
residue 136
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI5

44) chain A
residue 280
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI5

45) chain A
residue 480
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI5


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