eF-site ID 1t37-AP PDB Code 1t37 Chain A, P click to enlarge Title Design of specific inhibitors of phospholipase A2: Crystal structure of the complex formed between group I phospholipase A2 and a designed pentapeptide Leu-Ala-Ile-Tyr-Ser at 2.6A resolution Classification HYDROLASE Compound Phospholipase A2 isoform 3 Source ORGANISM_SCIENTIFIC: Naja sagittifera; Sequence A:  NLYQFKNMIQCTVPSRSWADFADYGCYCGKGGSGTPVDDL DRCCQTHDNCYNEAENISGCRPYFKTYSYECTQGTLTCKG DNNACAASVCDCDRLAAICFAGAPYNDDNYNIDLKARCN P:  LAIYS Description Functional site 1) chain A residue 54 type sequence E description BINDING SITE FOR RESIDUE ACT A 121 source : AC1 2) chain A residue 66 type sequence K description BINDING SITE FOR RESIDUE ACT A 121 source : AC1 3) chain A residue 67 type sequence T description BINDING SITE FOR RESIDUE ACT A 121 source : AC1 4) chain A residue 36 type sequence T description BINDING SITE FOR RESIDUE ACT A 122 source : AC2 5) chain A residue 62 type sequence R description BINDING SITE FOR RESIDUE ACT A 122 source : AC2 6) chain A residue 74 type sequence Q description BINDING SITE FOR RESIDUE ACT A 122 source : AC2 7) chain A residue 3 type sequence Y description BINDING SITE FOR RESIDUE ACT A 123 source : AC3 8) chain A residue 112 type sequence N description BINDING SITE FOR RESIDUE ACT A 123 source : AC3 9) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR source Swiss-Prot : SWS_FT_FI2 10) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR source Swiss-Prot : SWS_FT_FI2 11) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR source Swiss-Prot : SWS_FT_FI2 12) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR source Swiss-Prot : SWS_FT_FI2 13) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:15823962 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 94 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:15823962 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 44-51 type prosite sequence CCQTHDNC description PA2_HIS Phospholipase A2 histidine active site. CCQtHDnC source prosite : PS00118 16) chain A residue 90-100 type prosite sequence VCDCDRLAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC source prosite : PS00119

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