eF-site ID 2j50-B
PDB Code 2j50
Chain B

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Title Structure of Aurora-2 in complex with PHA-739358
Classification TRANSFERASE
Compound SERINE/THREONINE-PROTEIN KINASE 6
Source (STK6_HUMAN)
Sequence B:  WALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKA
QLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVY
LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYC
HSKRVIHRDIKPENLLLGSAGELKIADFGWSVTLCGTLDY
LPPEMIEDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYK
RISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLE
HPWITANSSK
Description (1)  SERINE/THREONINE-PROTEIN KINASE 6 (E.C.2.7.11.1)


Functional site

1) chain B
residue 142
type
sequence G
description BINDING SITE FOR RESIDUE SO4 B 1391
source : AC2

2) chain B
residue 143
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 1391
source : AC2

3) chain B
residue 144
type
sequence F
description BINDING SITE FOR RESIDUE SO4 B 1391
source : AC2

4) chain B
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 1391
source : AC2

5) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

6) chain B
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

7) chain B
residue 194
type
sequence L
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

8) chain B
residue 211
type
sequence E
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

9) chain B
residue 212
type
sequence Y
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

10) chain B
residue 213
type
sequence A
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

11) chain B
residue 214
type
sequence P
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

12) chain B
residue 215
type
sequence L
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

13) chain B
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

14) chain B
residue 260
type
sequence E
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

15) chain B
residue 275
type
sequence F
description BINDING SITE FOR RESIDUE 627 B 1390
source : AC4

16) chain B
residue 256
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
source Swiss-Prot : SWS_FT_FI1

17) chain B
residue 274
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 143
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 162
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 211
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 260
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
source Swiss-Prot : SWS_FT_FI2

22) chain B
residue 288
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 342
type MOD_RES
sequence S
description Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
source Swiss-Prot : SWS_FT_FI5

24) chain B
residue 258
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI6


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