eF-site ID 4dfr-A
PDB Code 4dfr
Chain A

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Title CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE
Classification OXIDOREDUCTASE
Compound DIHYDROFOLATE REDUCTASE
Source Escherichia coli (strain K12) (DYR_ECOLI)
Sequence A:  MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPV
IMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVE
GDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFKILERR
Description


Functional site

1) chain A
residue 5
type
sequence I
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

2) chain A
residue 6
type
sequence A
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

3) chain A
residue 7
type
sequence A
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

4) chain A
residue 22
type
sequence W
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

5) chain A
residue 27
type
sequence D
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

6) chain A
residue 28
type
sequence L
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

7) chain A
residue 31
type
sequence F
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

8) chain A
residue 94
type
sequence I
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

9) chain A
residue 113
type
sequence T
description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS.
source : APT

10) chain A
residue 49
type
sequence S
description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR
source : ANM

11) chain A
residue 28
type
sequence L
description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
source : AAB

12) chain A
residue 31
type
sequence F
description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
source : AAB

13) chain A
residue 50
type
sequence I
description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
source : AAB

14) chain A
residue 52
type
sequence R
description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
source : AAB

15) chain A
residue 54
type
sequence L
description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR
source : AAB

16) chain A
residue 28
type
sequence L
description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
source : AGL

17) chain A
residue 31
type
sequence F
description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
source : AGL

18) chain A
residue 32
type
sequence K
description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
source : AGL

19) chain A
residue 54
type
sequence L
description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
source : AGL

20) chain A
residue 57
type
sequence R
description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR
source : AGL

21) chain A
residue 43
type
sequence G
description BINDING SITE FOR RESIDUE CL A 160
source : AC1

22) chain A
residue 45
type
sequence H
description BINDING SITE FOR RESIDUE CL A 160
source : AC1

23) chain A
residue 46
type
sequence T
description BINDING SITE FOR RESIDUE CL A 160
source : AC1

24) chain A
residue 96
type
sequence G
description BINDING SITE FOR RESIDUE CL A 160
source : AC1

25) chain A
residue 5
type
sequence I
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

26) chain A
residue 6
type
sequence A
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

27) chain A
residue 27
type
sequence D
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

28) chain A
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

29) chain A
residue 32
type
sequence K
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

30) chain A
residue 52
type
sequence R
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

31) chain A
residue 57
type
sequence R
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

32) chain A
residue 94
type
sequence I
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

33) chain A
residue 100
type
sequence Y
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

34) chain A
residue 113
type
sequence T
description BINDING SITE FOR RESIDUE MTX A 161
source : AC4

35) chain A
residue 5
type BINDING
sequence I
description BINDING => ECO:0000305|PubMed:9012674
source Swiss-Prot : SWS_FT_FI1

36) chain A
residue 27
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:9012674
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 52
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:9012674
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 57
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:9012674
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 113
type BINDING
sequence T
description BINDING => ECO:0000305|PubMed:9012674
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 7
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 13
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 45
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 63
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 76
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 95
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19374017
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 13-35
type prosite
sequence VIGMENAMPWNLPADLAWFKRNT
description DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT
source prosite : PS00075


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