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

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Title Crystal Structure of Human Dihydropyrimidinease-like 2
Classification HYDROLASE
Compound Dihydropyrimidinase-related protein 2
Source Homo sapiens (Human) (DPYL2_HUMAN)
Sequence A:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG
VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK
AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD
YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF
QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD
LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK
VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN
WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC
TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK
MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP
DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL
EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA
B:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG
VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK
AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD
YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF
QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD
LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK
VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN
WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC
TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK
MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP
DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL
EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA
C:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG
VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK
AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD
YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF
QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD
LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK
VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN
WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC
TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK
MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP
DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL
EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLA
D:  DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGG
VKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTK
AALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCD
YSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRF
QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILD
LGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK
VMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKN
WAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHC
TFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGK
MDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP
DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVL
EDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAE
Description


Functional site

1) chain A
residue 81
type
sequence Q
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

2) chain A
residue 349
type
sequence T
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

3) chain B
residue 349
type
sequence T
description BINDING SITE FOR RESIDUE CA B 1001
source : AC2

4) chain C
residue 349
type
sequence T
description BINDING SITE FOR RESIDUE CA C 1002
source : AC3

5) chain D
residue 349
type
sequence T
description BINDING SITE FOR RESIDUE CA D 1003
source : AC4

6) chain A
residue 32
type MOD_RES
sequence Y
description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
source Swiss-Prot : SWS_FT_FI1

7) chain B
residue 32
type MOD_RES
sequence Y
description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
source Swiss-Prot : SWS_FT_FI1

8) chain C
residue 32
type MOD_RES
sequence Y
description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
source Swiss-Prot : SWS_FT_FI1

9) chain D
residue 32
type MOD_RES
sequence Y
description Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
source Swiss-Prot : SWS_FT_FI1

10) chain A
residue 258
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI2

11) chain B
residue 258
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI2

12) chain C
residue 258
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI2

13) chain D
residue 258
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47942
source Swiss-Prot : SWS_FT_FI3

15) chain B
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47942
source Swiss-Prot : SWS_FT_FI3

16) chain C
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47942
source Swiss-Prot : SWS_FT_FI3

17) chain D
residue 259
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47942
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 431
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI4

19) chain B
residue 431
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI4

20) chain C
residue 431
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI4

21) chain D
residue 431
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI4

22) chain A
residue 465
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI5

23) chain B
residue 465
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI5

24) chain C
residue 465
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI5

25) chain D
residue 465
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O08553
source Swiss-Prot : SWS_FT_FI5


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