eF-site ID 2v5q-ABCD
PDB Code 2v5q
Chain A, B, C, D

click to enlarge
Title CRYSTAL STRUCTURE OF WILD-TYPE PLK-1 KINASE DOMAIN IN COMPLEX WITH A SELECTIVE DARPIN
Classification TRANSFERASE
Compound SERINE/THREONINE-PROTEIN KINASE PLK1
Source (2V5Q)
Sequence A:  EIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEV
FAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHG
FFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLR
QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA
TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIG
CIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVA
ASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITC
LTIPP
B:  EIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEV
FAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHG
FFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLR
QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA
TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIG
CIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVA
ASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITC
LTIPP
C:  SDLGKKLLEAARAGQDDEVRILIANGADVNAVDNTGLTPL
HLAAVSGHLEIVEVLLKHGADVDAADVYGFTPLHLAAMTG
HLEIVEVLLKYGADVNAFDMTGSTPLHLAADEGHLEIVEV
LLKYGADVNA
D:  DLGKKLLEAARAGQDDEVRILIANGADVNAVDNTGLTPLH
LAAVSGHLEIVEVLLKHGADVDAADVYGFTPLHLAAMTGH
LEIVEVLLKYGADVNAFDMTGSTPLHLAADEGHLEIVEVL
LKYGADVNA
Description


Functional site

1) chain A
residue 176
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:18615013
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 176
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:18615013
source Swiss-Prot : SWS_FT_FI1

3) chain A
residue 59
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI2

4) chain B
residue 194
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

5) chain A
residue 82
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 131
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 178
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

8) chain A
residue 194
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 59
type BINDING
sequence L
description
source Swiss-Prot : SWS_FT_FI2

10) chain B
residue 82
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

11) chain B
residue 131
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

12) chain B
residue 178
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

13) chain A
residue 103
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18691976
source Swiss-Prot : SWS_FT_FI3

14) chain B
residue 103
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18691976
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 137
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:12207013
source Swiss-Prot : SWS_FT_FI4

16) chain B
residue 137
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:12207013
source Swiss-Prot : SWS_FT_FI4

17) chain A
residue 210
type MOD_RES
sequence T
description Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

18) chain B
residue 210
type MOD_RES
sequence T
description Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

19) chain A
residue 214
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI6

20) chain B
residue 214
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI6

21) chain A
residue 59-82
type prosite
sequence LGKGGFAKCFEISDADTKEVFAGK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFAKCFeIsdadtkev..........FAGK
source prosite : PS00107

22) chain A
residue 172-184
type prosite
sequence VIHRDLKLGNLFL
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKlgNLFL
source prosite : PS00108

23) chain A
residue 269
type MOD_RES
sequence S
description Phosphoserine; by autocatalysis => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

24) chain B
residue 269
type MOD_RES
sequence S
description Phosphoserine; by autocatalysis => ECO:0000250
source Swiss-Prot : SWS_FT_FI7


Display surface

Download
Links