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

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Title Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of the ATP complexation and glutaminase domain in catalytic coupling
Classification LIGASE
Compound Phosphoribosylformylglycinamidine synthase
Source ORGANISM_SCIENTIFIC: Salmonella enterica subsp. enterica serovar Typhimurium;
Sequence A:  GLVPRGSHMMEILRGSPALSAFRINKLLARFQAANLQVHN
IYAEYVHFADLNAPLNDSEQAQLTRLLQYGPALSSHTPAG
KLLLVTPRPGTISPWSSKATDIAHNCGLQQVDRLERGVAY
YIEASTLTAEQWRQVAAELHDRMMETVFSSLTDAEKLFIH
HQPAPVSSVDLLGEGRQALIDANLRLGLALAEDEIDYLQE
AFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGKP
QPKSLFKMIKNTFETTPDYVLSAYKDNAAVMEGSAVGRYF
ADHNTGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGS
GGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEED
FGKPERIVTALDIMTEGPLGGAAFNNEFGRPALTGYFRTY
EEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEIVV
GAKLIVLGGPAMNIGDFASVQRDNPEMERRCQEVIDRCWQ
LGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFELRDI
LSDEPGMSPLEIWCNESQERYVLAVAADQLPLFDELCKRE
RAPYAVIGDATEEQHLSLHDNHFDNQPIDLPLDVLLGKTP
KMTRDVQTLKAKGDALNRADITIADAVKRVLHLPTVAEKT
FLVTIGDRTVTGMVARDQMVGPWQVPVADCAVTTASLDSY
YGEAMSIGERAPVALLDFAASARLAVGEALTNIAATQIGD
IKRIKLSANWMAAAGHPGEDAGLYDAVKAVGEELCPQLGL
TIPVGKDSMSMKTRWQEGNEQREMTSPLSLVISAFARVED
VRHTLTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQL
GDKPADVRDVAQLKGFYDAMQALVAARKLLAWHDRSDGGL
LVTLAEMAFAGHCGVQVDIAALGDDHLAALFNEELGGVIQ
VRAEDRDAVEALLAQYGLADCVHYLGQALAGDRFVITAND
QTVFSESRTTLRVWWAETTWQMQRLRDNPQCADQEHEAKA
NDTDPGLNVKLSFDINEDIAAPYIATGARPKVAVLREQGV
NSHVEMAAAFHRAGFDAIDVHMSDLLGGRIGLGNFHALVA
CGGFSYGDVLGAGEGWAKSILFNHRVRDEFETFFHRPQTL
ALGVXNGCQMMSNLRELIPGSELWPRFVRNHSDRFEARFS
LVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDDAHLA
ALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTE
NGRVTIMMPHPERVFRTVANSWHPENWGEDSPWMRIFRNA
RKQLG
Description (1)  Phosphoribosylformylglycinamidine synthase (E.C.6.3.5.3)


Functional site

1) chain A
residue 219
type
sequence H
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

2) chain A
residue 222
type
sequence F
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

3) chain A
residue 258
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

4) chain A
residue 259
type
sequence N
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

5) chain A
residue 292
type
sequence K
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

6) chain A
residue 294
type
sequence E
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

7) chain A
residue 318
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

8) chain A
residue 502
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

9) chain A
residue 774
type
sequence V
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

10) chain A
residue 775
type
sequence G
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

11) chain A
residue 776
type
sequence K
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

12) chain A
residue 777
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 2001
source : AC1

13) chain A
residue 386
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

14) chain A
residue 387
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

15) chain A
residue 388
type
sequence Y
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

16) chain A
residue 389
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

17) chain A
residue 649
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

18) chain A
residue 668
type
sequence Q
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

19) chain A
residue 676
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

20) chain A
residue 678
type
sequence A
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

21) chain A
residue 679
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

22) chain A
residue 718
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

23) chain A
residue 722
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

24) chain A
residue 886
type
sequence S
description BINDING SITE FOR RESIDUE ADP A 2005
source : AC2

25) chain A
residue 718
type
sequence E
description BINDING SITE FOR RESIDUE MG A 2006
source : AC3

26) chain A
residue 886
type
sequence S
description BINDING SITE FOR RESIDUE MG A 2007
source : AC4

27) chain A
residue 679
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2008
source : AC5

28) chain A
residue 722
type
sequence N
description BINDING SITE FOR RESIDUE MG A 2008
source : AC5

29) chain A
residue 884
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2008
source : AC5

30) chain A
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 2002
source : AC6

31) chain A
residue 295
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 2002
source : AC6

32) chain A
residue 297
type
sequence N
description BINDING SITE FOR RESIDUE SO4 A 2002
source : AC6

33) chain A
residue 409
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 2002
source : AC6

34) chain A
residue 778
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 2002
source : AC6

35) chain A
residue 12
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 2009
source : AC7

36) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE SO4 A 2009
source : AC7

37) chain A
residue 14
type
sequence F
description BINDING SITE FOR RESIDUE SO4 A 2009
source : AC7

38) chain A
residue 998
type
sequence N
description BINDING SITE FOR RESIDUE SO4 A 2009
source : AC7

39) chain A
residue 1161
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 2009
source : AC7

40) chain A
residue 1135
type ACT_SITE
sequence X
description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00419
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 1260
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 1262
type ACT_SITE
sequence E
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 307
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00419
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 386
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 678
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI4

46) chain A
residue 886
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 679
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728
source Swiss-Prot : SWS_FT_FI5

48) chain A
residue 718
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728
source Swiss-Prot : SWS_FT_FI5

49) chain A
residue 722
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728
source Swiss-Prot : SWS_FT_FI5

50) chain A
residue 884
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728
source Swiss-Prot : SWS_FT_FI5


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