eF-site ID 2phi-AB
PDB Code 2phi
Chain A, B

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Title A LARGE CONFORMATIONAL CHANGE IS FOUND IN THE CRYSTAL STRUCTURE OF THE PORCINE PANCREATIC PHOSPHOLIPASE A2 POINT MUTANT F63V
Classification HYDROLASE (CARBOXYLIC ESTER)
Compound PHOSPHOLIPASE A2
Source Sus scrofa (Pig) (PA21B_PIG)
Sequence A:  ALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDE
LDRCCETHDNCYRDAKNLDSCKVLVDNPYTESYSYSCSNT
EITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDT
KKYC
B:  ALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDE
LDRCCETHDNCYRDAKNLDSCKVLVDNPYTESYSYSCSNT
EITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDT
KKYC
Description (1)  PHOSPHOLIPASE A2 (PHOSPHATIDE-2-ACYL-HYDROLASE) (E.C.3.1.1.4) MUTANT WITH PHE 63 REPLACED BY VAL (F63V)


Functional site

1) chain A
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CA A 125
source : AC1

2) chain A
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA A 125
source : AC1

3) chain A
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA A 125
source : AC1

4) chain A
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE CA A 125
source : AC1

5) chain A
residue 71
type
sequence E
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

6) chain A
residue 72
type
sequence S
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

7) chain A
residue 92
type
sequence E
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

8) chain B
residue 71
type
sequence E
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

9) chain B
residue 72
type
sequence S
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

10) chain B
residue 92
type
sequence E
description BINDING SITE FOR RESIDUE CA B 125
source : AC2

11) chain B
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 126
source : AC3

12) chain B
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA B 126
source : AC3

13) chain B
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA B 126
source : AC3

14) chain B
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE CA B 126
source : AC3

15) chain A
residue 28
type catalytic
sequence Y
description 83
source MCSA : MCSA1

16) chain A
residue 30
type catalytic
sequence G
description 83
source MCSA : MCSA1

17) chain A
residue 32
type catalytic
sequence G
description 83
source MCSA : MCSA1

18) chain A
residue 48
type catalytic
sequence H
description 83
source MCSA : MCSA1

19) chain A
residue 49
type catalytic
sequence D
description 83
source MCSA : MCSA1

20) chain A
residue 52
type catalytic
sequence Y
description 83
source MCSA : MCSA1

21) chain A
residue 73
type catalytic
sequence Y
description 83
source MCSA : MCSA1

22) chain A
residue 99
type catalytic
sequence D
description 83
source MCSA : MCSA1

23) chain B
residue 28
type catalytic
sequence Y
description 83
source MCSA : MCSA2

24) chain B
residue 30
type catalytic
sequence G
description 83
source MCSA : MCSA2

25) chain B
residue 32
type catalytic
sequence G
description 83
source MCSA : MCSA2

26) chain B
residue 48
type catalytic
sequence H
description 83
source MCSA : MCSA2

27) chain B
residue 49
type catalytic
sequence D
description 83
source MCSA : MCSA2

28) chain B
residue 52
type catalytic
sequence Y
description 83
source MCSA : MCSA2

29) chain B
residue 73
type catalytic
sequence Y
description 83
source MCSA : MCSA2

30) chain B
residue 99
type catalytic
sequence D
description 83
source MCSA : MCSA2

31) chain A
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 30
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 32
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 49
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 30
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 32
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 49
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00593
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 56
type LIPID
sequence K
description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336
source Swiss-Prot : SWS_FT_FI3

40) chain B
residue 56
type LIPID
sequence K
description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 48
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000269|PubMed:6876174
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 99
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000269|PubMed:6876174
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 48
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000269|PubMed:6876174
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 99
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000269|PubMed:6876174
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 44-51
type prosite
sequence CCETHDNC
description PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC
source prosite : PS00118

46) chain A
residue 95-105
type prosite
sequence ICNCDRNAAIC
description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC
source prosite : PS00119


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