eF-site ID 2j4z-B
PDB Code 2j4z
Chain B

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Title Structure of Aurora-2 in complex with PHA-680626
Classification TRANSFERASE
Compound SERINE THREONINE-PROTEIN KINASE 6
Source (STK6_HUMAN)
Sequence B:  RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF
KAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATR
VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALS
YCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR
RTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG
KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK
HNPSQRPMLREVLEHPWITANSSKPSNCQN
Description


Functional site

1) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

2) chain B
residue 194
type
sequence L
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

3) chain B
residue 210
type
sequence L
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

4) chain B
residue 211
type
sequence E
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

5) chain B
residue 212
type
sequence Y
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

6) chain B
residue 213
type
sequence A
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

7) chain B
residue 214
type
sequence P
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

8) chain B
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

9) chain B
residue 220
type
sequence R
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

10) chain B
residue 260
type
sequence E
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

11) chain B
residue 263
type
sequence L
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

12) chain B
residue 273
type
sequence A
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

13) chain B
residue 280
type
sequence H
description BINDING SITE FOR RESIDUE 626 B 1395
source : AC4

14) chain B
residue 247
type
sequence C
description BINDING SITE FOR RESIDUE ARS B 1396
source : AC5

15) chain B
residue 255
type
sequence R
description BINDING SITE FOR RESIDUE ARS B 1396
source : AC5

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

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

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

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

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

21) chain B
residue 287
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
source Swiss-Prot : SWS_FT_FI3

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

25) 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


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