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