eF-site ID 1b5o-AB
PDB Code 1b5o
Chain A, B

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Title THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1
Classification TRANSFERASE
Compound PROTEIN (ASPARTATE AMINOTRANSFERASE)
Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (AAT_THET8)
Sequence A:  MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGE
PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK
FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV
LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA
ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG
WRIGYACGPKEVIKAMASVSSQSTTSPDTIAQWATLEALT
NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA
FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV
RLSYATSEENLRKALERFARVL
B:  MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGE
PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK
FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV
LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA
ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG
WRIGYACGPKEVIKAMASVSSQSTTSPDTIAQWATLEALT
NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA
FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV
RLSYATSEENLRKALERFARVL
Description


Functional site

1) chain A
residue 39
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 414
source : AC1

2) chain A
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE PO4 A 414
source : AC1

3) chain A
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 414
source : AC1

4) chain A
residue 322
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 A 414
source : AC1

5) chain A
residue 361
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 414
source : AC1

6) chain B
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE PO4 B 414
source : AC2

7) chain B
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 414
source : AC2

8) chain B
residue 322
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 B 414
source : AC2

9) chain B
residue 361
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 414
source : AC2

10) chain A
residue 99
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

11) chain A
residue 100
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

12) chain A
residue 101
type
sequence S
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

13) chain A
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

14) chain A
residue 171
type
sequence N
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

15) chain A
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

16) chain A
residue 203
type
sequence D
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

17) chain A
residue 205
type
sequence I
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

18) chain A
residue 206
type
sequence Y
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

19) chain A
residue 233
type
sequence A
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

20) chain A
residue 234
type
sequence K
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

21) chain A
residue 242
type
sequence R
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

22) chain B
residue 64
type
sequence Y
description BINDING SITE FOR RESIDUE PLP A 413
source : AC3

23) chain A
residue 64
type
sequence Y
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

24) chain B
residue 99
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

25) chain B
residue 100
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

26) chain B
residue 101
type
sequence S
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

27) chain B
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

28) chain B
residue 171
type
sequence N
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

29) chain B
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

30) chain B
residue 203
type
sequence D
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

31) chain B
residue 205
type
sequence I
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

32) chain B
residue 206
type
sequence Y
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

33) chain B
residue 233
type
sequence A
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

34) chain B
residue 234
type
sequence K
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

35) chain B
residue 242
type
sequence R
description BINDING SITE FOR RESIDUE PLP B 413
source : AC4

36) chain A
residue 39
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00509
source Swiss-Prot : SWS_FT_FI1

37) chain B
residue 39
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00509
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 12
type SITE
sequence K
description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275
source Swiss-Prot : SWS_FT_FI3

39) chain B
residue 12
type SITE
sequence K
description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 125
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 175
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 361
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 125
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 175
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 361
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1GCK
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 234
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4
source Swiss-Prot : SWS_FT_FI4

47) chain B
residue 234
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4
source Swiss-Prot : SWS_FT_FI4

48) chain A
residue 231-244
type prosite
sequence GAAKAFAMTGWRIG
description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GAAKafAMtGWRIG
source prosite : PS00105


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