eF-site ID 1ovk-A PDB Code 1ovk Chain A click to enlarge Title T4 Lysozyme Cavity Mutant L99A/M102Q Bound with N-Allyl-Aniline Classification HYDROLASE Compound Lysozyme Source null (LYS_BPT4) Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCAAINQVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YK Description Functional site 1) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE CL A 173 source : AC1 2) chain A residue 145 type sequence R description BINDING SITE FOR RESIDUE CL A 173 source : AC1 3) chain A residue 49 type sequence A description BINDING SITE FOR RESIDUE CL A 178 source : AC2 4) chain A residue 69 type sequence Q description BINDING SITE FOR RESIDUE CL A 178 source : AC2 5) chain A residue 136 type sequence S description BINDING SITE FOR RESIDUE CL A 178 source : AC2 6) chain A residue 137 type sequence R description BINDING SITE FOR RESIDUE CL A 178 source : AC2 7) chain A residue 140 type sequence N description BINDING SITE FOR RESIDUE CL A 178 source : AC2 8) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 168 source : AC3 9) chain A residue 75 type sequence V description BINDING SITE FOR RESIDUE BME A 168 source : AC3 10) chain A residue 76 type sequence R description BINDING SITE FOR RESIDUE BME A 168 source : AC3 11) chain A residue 79 type sequence L description BINDING SITE FOR RESIDUE BME A 168 source : AC3 12) chain A residue 88 type sequence Y description BINDING SITE FOR RESIDUE BME A 168 source : AC3 13) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE BME A 169 source : AC4 14) chain A residue 104 type sequence F description BINDING SITE FOR RESIDUE BME A 169 source : AC4 15) chain A residue 72 type sequence D description BINDING SITE FOR RESIDUE BME A 170 source : AC5 16) chain A residue 88 type sequence Y description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 17) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 18) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 19) chain A residue 103 type sequence V description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 20) chain A residue 111 type sequence V description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 21) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 22) chain A residue 118 type sequence L description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 23) chain A residue 121 type sequence L description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 24) chain A residue 153 type sequence F description BINDING SITE FOR RESIDUE NYL A 405 source : AC6 25) chain A residue 32 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 29) 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 30) 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 31) chain A residue 11 type catalytic sequence E description 921 source MCSA : MCSA1 32) chain A residue 20 type catalytic sequence D description 921 source MCSA : MCSA1

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