eF-site ID 1qth-AB PDB Code 1qth Chain A, B click to enlarge Title THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME Classification HYDROLASE Compound LYSOZYME Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRAMLINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YK B:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRAMLINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YK Description Functional site 1) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 2) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 3) chain B residue 11 type catalytic sequence E description 921 source MCSA : MCSA2 4) chain B residue 20 type catalytic sequence D description 921 source MCSA : MCSA2 5) chain A residue 11 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 11 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 20 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 20 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4

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