eF-site ID 4kcu-AB
PDB Code 4kcu
Chain A, B

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Title Pyruvate kinase (PYK) from Trypanosoma brucei soaked with D-Malate
Classification TRANSFERASE
Compound Pyruvate kinase 1
Source Trypanosoma brucei brucei (KPYK1_TRYBB)
Sequence A:  SQLEHNIGLSIFEPVAKHRANRIVCTIGPSTQSVEALKNL
MKSGMSVARMNFSHGSHEYHQTTINNVRAAAAELGLHIGI
ALDTKGPEIRTGLFKDGEVSFAPGDIVCVTTDPAYEKVGT
KEKFYIDYPQLTNAVRPGGSIYVDDGVMTLRVVSKEDDRT
LKCHVNNHHRLTDRRGINLPGCEVDLPAVSEKDRKDLEFG
VAQGVDMIFASFIRTAEQVREVRAALGEKGKDILIISKIE
NHQGVQNIDSIIEASNGIMVARGDLGVEIPAEKVCVAQMC
IISKCNVVGKPVICATQMLESMTSNPRPTRAEVSDVANAV
LNGADCVMLSGETAKGKYPNEVVQYMARICVEAQSATHDT
VMFNSIKNLQKIPMCPEEAVCSSAVASAFEVQAKAMLVLS
NTGRSARLISKYRPNCPIICVTTRLQTCRQLNVTRSVVSV
FYDAAKSGEDKDKEKRVKLGLDFAKKEKYASTGDVVVVVH
ADHSVKGYPNQTRLIYLP
B:  SQLEHNIGLSIFEPVAKHRANRIVCTIGPSTQSVEALKNL
MKSGMSVARMNFSHGSHEYHQTTINNVRAAAAELGLHIGI
ALDTKGPEIRTGLFKDGEVSFAPGDIVCVTTDPAYEKVGT
KEKFYIDYPQLTNAVRPGGSIYVDDGVMTLRVVSKEDDRT
LKCHVNNHHRLTDRRGINLPGCEVDLPAVSEKDRKDLEFG
VAQGVDMIFASFIRTAEQVREVRAALGEKGKDILIISKIE
NHQGVQNIDSIIEASNGIMVARGDLGVEIPAEKVCVAQMC
IISKCNVVGKPVICATQMLESMTSNPRPTRAEVSDVANAV
LNGADCVMLSGETAKGKYPNEVVQYMARICVEAQSATHDT
VMFNSIKNLQKIPMCPEEAVCSSAVASAFEVQAKAMLVLS
NTGRSARLISKYRPNCPIICVTTRLQTCRQLNVTRSVVSV
FYDAAKSGEDKDKEKRVKLGLDFAKKEKYASTGDVVVVVH
ADHSVKGYPNQTRLIYLP
Description


Functional site

1) chain A
residue 50
type BINDING
sequence R
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 52
type BINDING
sequence N
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

3) chain B
residue 54
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

4) chain B
residue 84
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

5) chain B
residue 85
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

6) chain B
residue 264
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

7) chain B
residue 265
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

8) chain B
residue 297
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

9) chain A
residue 52
type BINDING
sequence N
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

10) chain A
residue 54
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 84
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 85
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 264
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 265
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 297
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 50
type BINDING
sequence R
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 91
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P14618
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 91
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P14618
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 234-246
type prosite
sequence ILIISKIENHQGV
description PYRUVATE_KINASE Pyruvate kinase active site signature. IlIISKIENhQGV
source prosite : PS00110

20) chain A
residue 241
type BINDING
sequence E
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

21) chain B
residue 241
type BINDING
sequence E
description BINDING => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 239
type SITE
sequence K
description Transition state stabilizer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 239
type SITE
sequence K
description Transition state stabilizer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4


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