eF-site ID 1gp7-ABC
PDB Code 1gp7
Chain A, B, C

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Title Acidic Phospholipase A2 from venom of Ophiophagus Hannah
Classification HYDROLASE
Compound PHOSPHOLIPASE A2
Source ORGANISM_COMMON: KING COBRA; ORGANISM_SCIENTIFIC: OPHIOPHAGUS HANNAH;
Sequence A:  HLIQFGNMIQCTVPGFLSWIKYADYGCYCGAGGSGTPVDK
LDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSER
TVTCKADNDECAAFICNCDRVAAHCFAASPYNNNNYNIDT
TTRC
B:  HLIQFGNMIQCTVPGFLSWIKYADYGCYCGAGGSGTPVDK
LDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSER
TVTCKADNDECAAFICNCDRVAAHCFAASPYNNNNYNIDT
TTRC
C:  HLIQFGNMIQCTVPGFLSWIKYADYGCYCGAGGSGTPVDK
LDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSER
TVTCKADNDECAAFICNCDRVAAHCFAASPYNNNNYNIDT
TTRC
Description


Functional site

1) chain A
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CA A1125
source : AC1

2) chain A
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA A1125
source : AC1

3) chain A
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA A1125
source : AC1

4) chain A
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE CA A1125
source : AC1

5) chain B
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CA B1125
source : AC2

6) chain B
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA B1125
source : AC2

7) chain B
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA B1125
source : AC2

8) chain B
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE CA B1125
source : AC2

9) chain C
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CA C1125
source : AC3

10) chain C
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE CA C1125
source : AC3

11) chain C
residue 32
type
sequence G
description BINDING SITE FOR RESIDUE CA C1125
source : AC3

12) chain C
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE CA C1125
source : AC3

13) chain A
residue 44-51
type prosite
sequence CCQVHDNC
description PA2_HIS Phospholipase A2 histidine active site. CCQvHDnC
source prosite : PS00118

14) chain A
residue 95-105
type prosite
sequence ICNCDRVAAHC
description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRVAaHC
source prosite : PS00119

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

16) chain A
residue 99
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

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

18) chain B
residue 99
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

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

20) chain C
residue 99
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250|UniProtKB:P14418
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

22) chain C
residue 30
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

23) chain C
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

24) chain C
residue 49
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 30
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 49
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 30
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 32
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 49
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2

32) chain C
residue 28
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:12217659, ECO:0007744|PDB:1GP7
source Swiss-Prot : SWS_FT_FI2


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