eF-site ID 1ijl-AB
PDB Code 1ijl
Chain A, B

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Title Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus
Classification HYDROLASE
Compound PHOSPHOLIPASE A2
Source ORGANISM_COMMON: Chinese moccasin; ORGANISM_SCIENTIFIC: Deinagkistrodon acutus;
Sequence A:  SLIQFETLIMKVVKKSGMFWYSAYGCYCGWGGHGRPQDAT
DRCCFVHDCCYGKVTGCDPKMDSYTYSEENGDIVCGGDDP
CKREICECDRVAADCFRDNLDTYNSDTYWRYPRQDCEESP
EPC
B:  SLIQFETLIMKVVKKSGMFWYSAYGCYCGWGGHGRPQDAT
DRCCFVHDCCYGKVTGCDPKMDSYTYSEENGDIVCGGDDP
CKREICECDRVAADCFRDNLDTYNSDTYWRYPRQDCEESP
EPC
Description


Functional site

1) chain A
residue 33
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

2) chain B
residue 27
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 202
source : AC2

3) chain B
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE CA B 202
source : AC2

4) chain B
residue 31
type
sequence G
description BINDING SITE FOR RESIDUE CA B 202
source : AC2

5) chain B
residue 48
type
sequence D
description BINDING SITE FOR RESIDUE CA B 202
source : AC2

6) chain A
residue 27
type
sequence Y
description BINDING SITE FOR RESIDUE CA A 203
source : AC3

7) chain A
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE CA A 203
source : AC3

8) chain A
residue 31
type
sequence G
description BINDING SITE FOR RESIDUE CA A 203
source : AC3

9) chain A
residue 48
type
sequence D
description BINDING SITE FOR RESIDUE CA A 203
source : AC3

10) chain A
residue 43-50
type prosite
sequence CCFVHDCC
description PA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
source prosite : PS00118

11) chain A
residue 85-95
type prosite
sequence ICECDRVAADC
description PA2_ASP Phospholipase A2 aspartic acid active site. ICECDRVAaDC
source prosite : PS00119

12) chain A
residue 47
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 89
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 47
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 89
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 27
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 29
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 31
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 27
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 29
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 31
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 48
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11752784
source Swiss-Prot : SWS_FT_FI3

23) chain B
residue 48
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11752784
source Swiss-Prot : SWS_FT_FI3


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