eF-site ID 5lzm-A PDB Code 5lzm Chain A click to enlarge Title COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS Classification HYDROLASE (O-GLYCOSYL) Compound T4 LYSOZYME Source (LYS_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YK Description (1)  LYSOZYME (E.C.3.2.1.17) (MEDIUM SALT) Functional site 1) chain A residue 142 type sequence T description BINDING SITE FOR RESIDUE CL A 173 source : AC1 2) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE CL A 173 source : AC1 3) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE CL A 173 source : AC1 4) chain A residue 52 type sequence R description BINDING SITE FOR RESIDUE BME A 179 source : AC3 5) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE BME A 179 source : AC3 6) chain A residue 54 type sequence C description BINDING SITE FOR RESIDUE BME A 179 source : AC3 7) chain A residue 57 type sequence V description BINDING SITE FOR RESIDUE BME A 179 source : AC3 8) chain A residue 58 type sequence I description BINDING SITE FOR RESIDUE BME A 179 source : AC3 9) chain A residue 59 type sequence T description BINDING SITE FOR RESIDUE BME A 179 source : AC3 10) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE BME A 179 source : AC3 11) chain A residue 3 type sequence I description BINDING SITE FOR RESIDUE BME A 180 source : AC4 12) chain A residue 68 type sequence N description BINDING SITE FOR RESIDUE BME A 180 source : AC4 13) chain A residue 93 type sequence A description BINDING SITE FOR RESIDUE BME A 180 source : AC4 14) chain A residue 97 type sequence C description BINDING SITE FOR RESIDUE BME A 180 source : AC4 15) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 900 source : AC5 16) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 17) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 18) 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 19) 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 20) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4

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