eF-site ID 6fm0-AB
PDB Code 6fm0
Chain A, B

click to enlarge
Title Deoxyguanylosuccinate synthase (DgsS) and ATP structure at 1.7 Angstrom resolution
Classification BIOSYNTHETIC PROTEIN
Compound Adenylosuccinate synthetase
Source (G3FFN6_9CAUD)
Sequence A:  ENVDLVIDLQFGSTGKGLIAGYLAEKNGYDTVINANMPNA
GHTYINAEGRKWMHKVLPNGIVSPNLKRVMLGAGSVFSIN
RLMEEIEMSKDLLHDKVAILIHPMATVLDSMAAMVEKLQR
DPTNNTIVARDVAQYDGRIAQYVCTVEEWDMALMASERIL
AEGAQGFSLSLNQEFYPYCTSRDCTPARFLADMGIPLPML
NKVIGTARCHPIRGHYPDQEERVFSFSFIQMQKAMWTCQP
DEVFLNFCNYLSPMGWQDIVHQIEVAAQSRYCDAEVKYLG
FGPTFNDVELREDV
B:  ENVDLVIDLQFGSTGKGLIAGYLAEKNGYDTVINANMPNA
GHTYINAEGRKWMHKVLPNGIVSPNLKRVMLGAGSVFSIN
RLMEEIEMSKDLLHDKVAILIHPMATVLDGSMAAMVEKLQ
RDPTNNTIVARDVAQYDGRIAQYVCTVEEWDMALMASERI
LAEGAQGFSLSLNQEFYPYCTSRDCTPARFLADMGIPLPM
LNKVIGTARCHPIRVGHYPDQEERRVFSFSFIQMQKAMWT
CQPDEVFLNFCNYLSPQDIVHQIEVAAQSRYCDAEVKYLG
FGPTFNDVEL
Description (1)  Adenylosuccinate synthetase


Functional site

1) chain A
residue 14
type
sequence S
description binding site for residue ATP A 401
source : AC1

2) chain A
residue 15
type
sequence T
description binding site for residue ATP A 401
source : AC1

3) chain A
residue 16
type
sequence G
description binding site for residue ATP A 401
source : AC1

4) chain A
residue 17
type
sequence K
description binding site for residue ATP A 401
source : AC1

5) chain A
residue 18
type
sequence G
description binding site for residue ATP A 401
source : AC1

6) chain A
residue 43
type
sequence H
description binding site for residue ATP A 401
source : AC1

7) chain A
residue 294
type
sequence N
description binding site for residue ATP A 401
source : AC1

8) chain A
residue 295
type
sequence F
description binding site for residue ATP A 401
source : AC1

9) chain A
residue 297
type
sequence N
description binding site for residue ATP A 401
source : AC1

10) chain A
residue 330
type
sequence G
description binding site for residue ATP A 401
source : AC1

11) chain A
residue 331
type
sequence P
description binding site for residue ATP A 401
source : AC1

12) chain B
residue 13
type
sequence G
description binding site for residue ATP B 401
source : AC2

13) chain B
residue 14
type
sequence S
description binding site for residue ATP B 401
source : AC2

14) chain B
residue 16
type
sequence G
description binding site for residue ATP B 401
source : AC2

15) chain B
residue 17
type
sequence K
description binding site for residue ATP B 401
source : AC2

16) chain B
residue 43
type
sequence H
description binding site for residue ATP B 401
source : AC2

17) chain B
residue 44
type
sequence T
description binding site for residue ATP B 401
source : AC2

18) chain B
residue 187
type
sequence Q
description binding site for residue ATP B 401
source : AC2

19) chain B
residue 295
type
sequence F
description binding site for residue ATP B 401
source : AC2

20) chain B
residue 330
type
sequence G
description binding site for residue ATP B 401
source : AC2

21) chain A
residue 14
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04166, ECO:0000305|PubMed:33926954
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 14
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04166, ECO:0000305|PubMed:33926954
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 14
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 142
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 187
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 202
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 294
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 297
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 330
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 14
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 15
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 15
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 16
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 17
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 18
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 40
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 42
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 43
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 44
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 16
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 142
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 187
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 202
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 294
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 297
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 330
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 17
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 18
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 40
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 42
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 43
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 44
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6FM1
source Swiss-Prot : SWS_FT_FI2

53) chain B
residue 269
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:33926955, ECO:0007744|PDB:6TNH
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links