eF-site ID 1g2x-ABC
PDB Code 1g2x
Chain A, B, C

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Title Sequence induced trimerization of krait PLA2: crystal structure of the trimeric form of krait PLA2
Classification TOXIN
Compound PHOSPHOLIPASE A2
Source ORGANISM_SCIENTIFIC: Bungarus caeruleus;
Sequence A:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD
RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT
ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ
B:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD
RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT
ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ
C:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD
RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT
ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ
Description


Functional site

1) chain A
residue 44-51
type prosite
sequence CCYTHDHC
description PA2_HIS Phospholipase A2 histidine active site. CCYtHDhC
source prosite : PS00118

2) chain A
residue 90-100
type prosite
sequence LCDCDRTAAIC
description PA2_ASP Phospholipase A2 aspartic acid active site. LCDCDRTAaIC
source prosite : PS00119

3) chain A
residue 48
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

4) chain A
residue 94
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

5) chain B
residue 48
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

6) chain B
residue 94
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

7) chain C
residue 48
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

8) chain C
residue 94
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

9) chain A
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

10) chain C
residue 30
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

11) chain C
residue 32
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

12) chain C
residue 49
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

13) chain A
residue 30
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 32
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 49
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

16) chain B
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

17) chain B
residue 30
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 32
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 49
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI2


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