eF-site ID 1a2a-ABCDEFGH PDB Code 1a2a Chain A, B, C, D, E, F, G, H click to enlarge Title AGKISTROTOXIN, A PHOSPHOLIPASE A2-TYPE PRESYNAPTIC NEUROTOXIN FROM AGKISTRODON HALYS PALLAS Classification PRESYNAPTIC NEUROTOXIN Compound PHOSPHOLIPASE A2 Source ORGANISM_COMMON: halys viper; ORGANISM_SCIENTIFIC: Gloydius halys; Sequence A:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC B:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC C:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC D:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC E:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC F:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC G:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC H:  NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGNGKPKDGT DRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTN CEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSE EC Description Functional site 1) chain A residue 108 type sequence R description BINDING SITE FOR RESIDUE CL D 200 source : AC1 2) chain D residue 4 type sequence Q description BINDING SITE FOR RESIDUE CL D 200 source : AC1 3) chain D residue 75 type sequence Y description BINDING SITE FOR RESIDUE CL D 200 source : AC1 4) chain C residue 108 type sequence R description BINDING SITE FOR RESIDUE CL C 400 source : AC2 5) chain E residue 108 type sequence R description BINDING SITE FOR RESIDUE CL E 600 source : AC3 6) chain H residue 4 type sequence Q description BINDING SITE FOR RESIDUE CL E 600 source : AC3 7) chain F residue 4 type sequence Q description BINDING SITE FOR RESIDUE CL F 800 source : AC4 8) chain F residue 75 type sequence Y description BINDING SITE FOR RESIDUE CL F 800 source : AC4 9) chain G residue 108 type sequence R description BINDING SITE FOR RESIDUE CL F 800 source : AC4 10) chain A residue 44-51 type prosite sequence CCFVHDCC description PA2_HIS Phospholipase A2 histidine active site. CCFvHDcC source prosite : PS00118 11) chain A residue 95-105 type prosite sequence ICECDRVAAEC description PA2_ASP Phospholipase A2 aspartic acid active site. ICECDRVAaEC source prosite : PS00119 12) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 13) chain C residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 14) chain C residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 15) chain C residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 16) chain D residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 17) chain D residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 18) chain D residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 19) chain D residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 20) chain E residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 21) chain E residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 22) chain E residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 23) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 24) chain E residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 25) chain F residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 26) chain F residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 27) chain F residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 28) chain F residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 29) chain G residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 30) chain G residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 31) chain G residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 32) chain G residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 33) chain H residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 34) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 35) chain H residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 36) chain H residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 37) chain H residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 38) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 39) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 40) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 41) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 42) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 43) chain C residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10666574, ECO:0007744|PDB:1BJJ source Swiss-Prot : SWS_FT_FI2 44) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 46) chain F residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 47) chain F residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 48) chain G residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 49) chain G residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 50) chain H residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 51) chain H residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 53) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 57) chain D residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 58) chain D residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1 59) chain E residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:9733637 source Swiss-Prot : SWS_FT_FI1

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