eF-site ID 1g4i-A PDB Code 1g4i Chain A click to enlarge Title Crystal structure of the bovine pancreatic phospholipase A2 at 0.97A Classification HYDROLASE Compound PHOSPHOLIPASE A2 Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  ALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDD LDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNN EITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDK KNC Description Functional site 1) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA A 124 source : AC1 2) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE CA A 124 source : AC1 3) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE CA A 124 source : AC1 4) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE CA A 124 source : AC1 5) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE CL A 125 source : AC2 6) chain A residue 82 type sequence I description BINDING SITE FOR RESIDUE CL A 125 source : AC2 7) chain A residue 100 type sequence R description BINDING SITE FOR RESIDUE CL A 125 source : AC2 8) chain A residue 6 type sequence N description BINDING SITE FOR RESIDUE MRD A 127 source : AC3 9) chain A residue 22 type sequence F description BINDING SITE FOR RESIDUE MRD A 127 source : AC3 10) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE MRD A 127 source : AC3 11) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE MRD A 127 source : AC3 12) chain A residue 2 type sequence L description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 13) chain A residue 5 type sequence F description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 14) chain A residue 6 type sequence N description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 15) chain A residue 18 type sequence P description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 16) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 17) chain A residue 22 type sequence F description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 18) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 19) chain A residue 29 type sequence C description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 20) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 21) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE MRD A 128 source : AC4 22) chain A residue 15 type sequence S description BINDING SITE FOR RESIDUE MRD A 129 source : AC5 23) chain A residue 16 type sequence S description BINDING SITE FOR RESIDUE MRD A 129 source : AC5 24) chain A residue 21 type sequence D description BINDING SITE FOR RESIDUE MRD A 129 source : AC5 25) chain A residue 54 type sequence Q description BINDING SITE FOR RESIDUE MRD A 129 source : AC5 26) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE MPD A 126 source : AC6 27) chain A residue 31 type sequence L description BINDING SITE FOR RESIDUE MPD A 126 source : AC6 28) chain A residue 10 type sequence K description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 29) chain A residue 17 type sequence E description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 30) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 31) chain A residue 20 type sequence L description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 32) chain A residue 105 type sequence C description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 33) chain A residue 109 type sequence V description BINDING SITE FOR RESIDUE MPD A 130 source : AC7 34) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:7464926 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:7464926 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS source Swiss-Prot : SWS_FT_FI2 37) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS source Swiss-Prot : SWS_FT_FI2 38) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS source Swiss-Prot : SWS_FT_FI2 39) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS source Swiss-Prot : SWS_FT_FI2 40) chain A residue 44-51 type prosite sequence CCQTHDNC description PA2_HIS Phospholipase A2 histidine active site. CCQtHDnC source prosite : PS00118 41) 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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