eF-site ID 1g0z-A
PDB Code 1g0z
Chain A

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Title SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTION
Classification TOXIN
Compound PHOSPHOLIPASE A2
Source ORGANISM_SCIENTIFIC: Bungarus caeruleus;
Sequence A:  NLKQFKNMIQCAGTRTWTSYIGYGCYCGYGGSGTPVDELD
RCCYTHDHCYNKAANIPGCNPLIKTYSYTCTKPNITCNDT
SDSCARFICDCDRTAAICFASAPYNINNIMISASTSCQ
Description


Functional site

1) chain A
residue 82
type
sequence T
description BINDING SITE FOR RESIDUE CL A 121
source : AC2

2) chain A
residue 83
type
sequence S
description BINDING SITE FOR RESIDUE CL A 121
source : AC2

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

4) chain A
residue 90-100
type prosite
sequence ICDCDRTAAIC
description PA2_ASP Phospholipase A2 aspartic acid active site. ICDCDRTAaIC
source prosite : PS00119

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

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

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

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

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

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

11) chain A
residue 31
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:15721580
source Swiss-Prot : SWS_FT_FI3


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