eF-site ID 199l-A PDB Code 199l Chain A click to enlarge Title THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME Classification HYDROLASE (O-GLYCOSYL) Compound LYSOZYME Source (LYCV_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRM AQQKRWDEMAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YK Description Functional site 1) chain A residue 124 type sequence K description BINDING SITE FOR RESIDUE CL A 173 source : AC1 2) chain A residue 142 type sequence T description BINDING SITE FOR RESIDUE CL A 173 source : AC1 3) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE CL A 173 source : AC1 4) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE CL A 173 source : AC1 5) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 901 source : AC3 6) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 902 source : AC4 7) chain A residue 93 type sequence A description BINDING SITE FOR RESIDUE BME A 902 source : AC4 8) chain A residue 97 type sequence A description BINDING SITE FOR RESIDUE BME A 902 source : AC4 9) chain A residue 100 type sequence I description BINDING SITE FOR RESIDUE BME A 902 source : AC4 10) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 11) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1 12) 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 13) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 17) 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

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